Catalytic triad (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Catalytic triad" in English language version.

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84nih.gov

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1ebi.ac.uk

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cam.ac.uk

repository.cam.ac.uk

Shafee T (2014). Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity (PhD thesis). University of Cambridge. doi:10.17863/CAM.16528.

doi.org

Dodson G, Wlodawer A (1998). "Catalytic triads and their relatives". Trends Biochem. Sci. 23 (9): 347–52. doi:10.1016/S0968-0004(98)01254-7. PMID 9787641.
Buller AR, Townsend CA (2013). "Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad". Proc. Natl. Acad. Sci. U.S.A. 110 (8): E653–61. Bibcode:2013PNAS..110E.653B. doi:10.1073/pnas.1221050110. PMC 3581919. PMID 23382230.
Neurath H (1994). "Proteolytic enzymes past and present: the second golden era. Recollections, special section in honor of Max Perutz". Protein Sci. 3 (10): 1734–9. doi:10.1002/pro.5560031013. PMC 2142620. PMID 7849591.
Ohman KP, Hoffman A, Keiser HR (1990). "Endothelin-induced vasoconstriction and release of atrial natriuretic peptides in the rat". Acta Physiol. Scand. 138 (4): 549–56. doi:10.1111/j.1748-1716.1990.tb08883.x. PMID 2141214.
Dixon GH, Kauffman DL, Neurath H (1958). "Amino Acid Sequence in the Region of Diisopropyl Phosphoryl Binding in Dip-Trypsin". J. Am. Chem. Soc. 80 (5): 1260–1. doi:10.1021/ja01538a059.
Matthews BW, Sigler PB, Henderson R, et al. (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089): 652–656. Bibcode:1967Natur.214..652M. doi:10.1038/214652a0. PMID 6049071. S2CID 4273406.
Walsh KA, Neurath H (1964). "Trypsinogen and Chymotrypsinogen as Homologous Proteins". Proc. Natl. Acad. Sci. U.S.A. 52 (4): 884–9. Bibcode:1964PNAS...52..884W. doi:10.1073/pnas.52.4.884. PMC 300366. PMID 14224394.
de Haën C, Neurath H, Teller DC (1975). "The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships". J. Mol. Biol. 92 (2): 225–59. doi:10.1016/0022-2836(75)90225-9. PMID 1142424.
Lesk AM, Fordham WD (1996). "Conservation and variability in the structures of serine proteinases of the chymotrypsin family". J. Mol. Biol. 258 (3): 501–37. doi:10.1006/jmbi.1996.0264. PMID 8642605.
Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 (5178): 337–40. Bibcode:1969Natur.221..337B. doi:10.1038/221337a0. PMID 5764436. S2CID 4214520.
Gorbalenya AE, Blinov VM, Donchenko AP (1986). "Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families". FEBS Lett. 194 (2): 253–7. doi:10.1016/0014-5793(86)80095-3. PMID 3000829. S2CID 23268152.
Bazan JF, Fletterick RJ (1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications". Proc. Natl. Acad. Sci. U.S.A. 85 (21): 7872–6. Bibcode:1988PNAS...85.7872B. doi:10.1073/pnas.85.21.7872. PMC 282299. PMID 3186696.
Phan J, Zdanov A, Evdokimov AG, et al. (2002). "Structural basis for the substrate specificity of tobacco etch virus protease". J. Biol. Chem. 277 (52): 50564–72. doi:10.1074/jbc.M207224200. PMID 12377789.
Rawlings ND, Barrett AJ (1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. doi:10.1042/bj2900205. PMC 1132403. PMID 8439290.
Rawlings ND, Barrett AJ, Bateman A (2010). "MEROPS: the peptidase database". Nucleic Acids Res. 38 (supl_1): D227–33. doi:10.1093/nar/gkp971. PMC 2808883. PMID 19892822.
Frey PA, Whitt SA, Tobin JB (1994). "A low-barrier hydrogen bond in the catalytic triad of serine proteases". Science. 264 (5167): 1927–30. Bibcode:1994Sci...264.1927F. doi:10.1126/science.7661899. PMID 7661899.
Ash EL, Sudmeier JL, De Fabo EC, et al. (1997). "A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment". Science. 278 (5340): 1128–32. Bibcode:1997Sci...278.1128A. doi:10.1126/science.278.5340.1128. PMID 9353195.
Agback P, Agback T (2018). "Direct evidence of a low barrier hydrogen bond in the catalytic triad of a Serine protease". Sci. Rep. 8 (1): 10078. Bibcode:2018NatSR...810078A. doi:10.1038/s41598-018-28441-7. PMC 6031666. PMID 29973622.
Schutz CN, Warshel A (2004). "The low barrier hydrogen bond (LBHB) proposal revisited: the case of the Asp... His pair in serine proteases". Proteins. 55 (3): 711–23. doi:10.1002/prot.20096. PMID 15103633. S2CID 34229297.
Warshel A, Papazyan A (1996). "Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13665–70. Bibcode:1996PNAS...9313665W. doi:10.1073/pnas.93.24.13665. PMC 19385. PMID 8942991.
Fersht, A.R.; Requena, Y (1971). "Mechanism of the Chymotrypsin-Catalyzed Hydrolysis of Amides. pH Dependence of kc and Km.' Kinetic Detection of an Intermediate". J. Am. Chem. Soc. 93 (25): 7079–87. doi:10.1021/ja00754a066. PMID 5133099.
Zeeberg, B; Caswell, M; Caplow, M (1973). "Concerning a reported change in rate-determining step in chymotrypsin catalysis". J. Am. Chem. Soc. 95 (8): 2734–5. doi:10.1021/ja00789a081. PMID 4694533.
Shafee T (2014). Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity (PhD thesis). University of Cambridge. doi:10.17863/CAM.16528.
Ekici OD, Paetzel M, Dalbey RE (2008). "Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration". Protein Sci. 17 (12): 2023–37. doi:10.1110/ps.035436.108. PMC 2590910. PMID 18824507.
McGrath ME, Wilke ME, Higaki JN, et al. (1989). "Crystal structures of two engineered thiol trypsins". Biochemistry. 28 (24): 9264–70. doi:10.1021/bi00450a005. PMID 2611228.
Polgár L, Asbóth B (1986). "The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state". J. Theor. Biol. 121 (3): 323–6. Bibcode:1986JThBi.121..323P. doi:10.1016/s0022-5193(86)80111-4. PMID 3540454.
Brandt W, Wessjohann LA (2005). "The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state". ChemBioChem. 6 (2): 386–94. doi:10.1002/cbic.200400276. PMID 15651042. S2CID 25575160.
Damblon C, Raquet X, Lian LY, et al. (1996). "The catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1747–52. Bibcode:1996PNAS...93.1747D. doi:10.1073/pnas.93.5.1747. PMC 39852. PMID 8700829.
Jelsch C, Lenfant F, Masson JM, et al. (1992). "Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution". FEBS Lett. 299 (2): 135–42. doi:10.1016/0014-5793(92)80232-6. PMID 1544485.
Brannigan JA, Dodson G, Duggleby HJ, et al. (1995). "A protein catalytic framework with an N-terminal nucleophile is capable of self-activation". Nature. 378 (6555): 416–9. Bibcode:1995Natur.378..416B. doi:10.1038/378416a0. PMID 7477383. S2CID 4277904.
Cheng H, Grishin NV (2005). "DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain". Protein Sci. 14 (7): 1902–10. doi:10.1110/ps.051364905. PMC 2253344. PMID 15937278.
Sun Y, Yin S, Feng Y, et al. (2014). "Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad". J. Biol. Chem. 289 (22): 15867–79. doi:10.1074/jbc.m113.535641. PMC 4140940. PMID 24737327.
Rauwerdink A, Kazlauskas RJ (2015). "How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes". ACS Catal. 5 (10): 6153–6176. doi:10.1021/acscatal.5b01539. PMC 5455348. PMID 28580193.
Sinha, P., & Yadav, A. K. (2023). In silico identification of cyclosporin derivatives as potential inhibitors for RdRp of rotavirus by molecular docking and molecular dynamic studies. Journal of Biomolecular Structure and Dynamics, 42(10), 5001–5014. https://doi.org/10.1080/07391102.2023.2239918
Beveridge AJ (1996). "A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinases". Protein Sci. 5 (7): 1355–65. doi:10.1002/pro.5560050714. PMC 2143470. PMID 8819168.
Allen MD, Buchberger A, Bycroft M (2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". J. Biol. Chem. 281 (35): 25502–8. doi:10.1074/jbc.M601173200. PMID 16807242.
Sanchez-Pulido L, Ponting CP (2016). "Vasohibins: new transglutaminase-like cysteine proteases possessing a non-canonical Cys-His-Ser catalytic triad". Bioinformatics. 32 (10): 1441–5. doi:10.1093/bioinformatics/btv761. PMC 4866520. PMID 26794318.
Sato Y, Sonoda H (2007). "The vasohibin family: a negative regulatory system of angiogenesis genetically programmed in endothelial cells". Arterioscler. Thromb. Vasc. Biol. 27 (1): 37–41. doi:10.1161/01.atv.0000252062.48280.61. PMID 17095714.
Shin S, Yun YS, Koo HM, et al. (2003). "Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad". J. Biol. Chem. 278 (27): 24937–43. doi:10.1074/jbc.M302156200. PMID 12711609.
Cerqueira NM, Moorthy H, Fernandes PA, et al. (2017). "The mechanism of the Ser-(cis)Ser-Lys catalytic triad of peptide amidases". Phys. Chem. Chem. Phys. 19 (19): 12343–12354. Bibcode:2017PCCP...1912343C. doi:10.1039/C7CP00277G. PMID 28453015. Archived from the original on 2017-12-24. Retrieved 2017-12-24.
Toscano MD, Woycechowsky KJ, Hilvert D (2007). "Minimalist active-site redesign: teaching old enzymes new tricks". Angew. Chem. 46 (18): 3212–36. doi:10.1002/anie.200604205. PMID 17450624.
Abrahmsén L, Tom J, Burnier J, et al. (1991). "Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution". Biochemistry. 30 (17): 4151–9. CiteSeerX 10.1.1.461.9606. doi:10.1021/bi00231a007. PMID 2021606.
Jackson DY, Burnier J, Quan C, et al. (1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183): 243–7. Bibcode:1994Sci...266..243J. doi:10.1126/science.7939659. JSTOR 2884761. PMID 7939659.
Syed R, Wu ZP, Hogle JM, et al. (1993). "Crystal structure of selenosubtilisin at 2.0-A resolution". Biochemistry. 32 (24): 6157–64. doi:10.1021/bi00075a007. PMID 8512925.
Mao S, Dong Z, Liu J, et al. (2005). "Semisynthetic tellurosubtilisin with glutathione peroxidase activity". J. Am. Chem. Soc. 127 (33): 11588–9. doi:10.1021/ja052451v. PMID 16104720.
Bouroushian M (2010). "Electrochemistry of the Chalcogens". Electrochemistry of Metal Chalcogenides. Monographs in Electrochemistry. Berlin, Heidelberg: Springer. pp. 57–75. doi:10.1007/978-3-642-03967-6_2. ISBN 9783642039669.
Shafee T, Gatti-Lafranconi P, Minter R, et al. (2015). "Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease". ChemBioChem. 16 (13): 1866–9. doi:10.1002/cbic.201500295. PMC 4576821. PMID 26097079.
Okochi N, Kato-Murai M, Kadonosono T, et al. (2007). "Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface". Appl. Microbiol. Biotechnol. 77 (3): 597–603. doi:10.1007/s00253-007-1197-0. PMID 17899065. S2CID 35590920.
Rajagopalan S, Wang C, Yu K, et al. (2014). "Design of activated serine-containing catalytic triads with atomic-level accuracy". Nat. Chem. Biol. 10 (5): 386–91. doi:10.1038/nchembio.1498. PMC 4048123. PMID 24705591.
Bhowmick D, Mugesh G (2015). "Introduction of a catalytic triad increases the glutathione peroxidase-like activity of diaryl diselenides". Org. Biomol. Chem. 13 (34): 9072–82. doi:10.1039/C5OB01294E. PMID 26220806.
Bhowmick D, Mugesh G (2015). "Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics". Org. Biomol. Chem. 13 (41): 10262–72. doi:10.1039/c5ob01665g. PMID 26372527.
Nothling MD, Ganesan A, Condic-Jurkic K, et al. (2017). "Simple Design of an Enzyme-Inspired Supported Catalyst Based on a Catalytic Triad". Chem. 2 (5): 732–745. Bibcode:2017Chem....2..732N. doi:10.1016/j.chempr.2017.04.004.
Gulseren G, Khalily MA, Tekinay AB, et al. (2016). "Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis". J. Mater. Chem. B. 4 (26): 4605–4611. doi:10.1039/c6tb00795c. hdl:11693/36666. PMID 32263403.
Halabi N, Rivoire O, Leibler S, et al. (2009). "Protein sectors: evolutionary units of three-dimensional structure". Cell. 138 (4): 774–86. doi:10.1016/j.cell.2009.07.038. PMC 3210731. PMID 19703402.
Murzin AG (1998). "How far divergent evolution goes in proteins". Current Opinion in Structural Biology. 8 (3): 380–387. doi:10.1016/S0959-440X(98)80073-0. PMID 9666335.
Gerlt JA, Babbitt PC (2001). "Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies". Annu. Rev. Biochem. 70 (1): 209–46. doi:10.1146/annurev.biochem.70.1.209. PMID 11395407.
Murphy JM, Farhan H, Eyers PA (2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochem. Soc. Trans. 45 (2): 537–544. doi:10.1042/bst20160400. PMID 28408493.
Stehle F, Brandt W, Stubbs MT, et al. (2009). "Sinapoyltransferases in the light of molecular evolution". Phytochemistry. Evolution of Metabolic Diversity. 70 (15–16): 1652–62. Bibcode:2009PChem..70.1652S. doi:10.1016/j.phytochem.2009.07.023. PMID 19695650.
Dimitriou PS, Denesyuk A, Takahashi S, et al. (2017). "Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families". Proteins. 85 (10): 1845–1855. doi:10.1002/prot.25338. PMID 28643343. S2CID 25363240.
Smith JL (1998). "Glutamine PRPP amidotransferase: snapshots of an enzyme in action". Current Opinion in Structural Biology. 8 (6): 686–94. doi:10.1016/s0959-440x(98)80087-0. PMID 9914248.
Smith JL, Zaluzec EJ, Wery JP, et al. (1994). "Structure of the allosteric regulatory enzyme of purine biosynthesis". Science. 264 (5164): 1427–33. Bibcode:1994Sci...264.1427S. doi:10.1126/science.8197456. PMID 8197456.
Fischer K, Reynolds SL (2015). "Pseudoproteases: mechanisms and function". Biochem. J. 468 (1): 17–24. doi:10.1042/BJ20141506. PMID 25940733.
Todd AE, Orengo CA, Thornton JM (2002). "Sequence and structural differences between enzyme and nonenzyme homologs". Structure. 10 (10): 1435–51. doi:10.1016/s0969-2126(02)00861-4. PMID 12377129.
Iversen LF, Kastrup JS, Bjørn SE, et al. (1997). "Structure of HBP, a multifunctional protein with a serine proteinase fold". Nat. Struct. Biol. 4 (4): 265–8. doi:10.1038/nsb0497-265. PMID 9095193. S2CID 19949043.
Zettl M, Adrain C, Strisovsky K, et al. (2011). "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling". Cell. 145 (1): 79–91. doi:10.1016/j.cell.2011.02.047. PMC 3149277. PMID 21439629.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759. PMID 27378062.
Cheng CY, Morris I, Bardin CW (1993). "Testins Are Structurally Related to the Mouse Cysteine Proteinase Precursor But Devoid of Any Protease/Anti-Protease Activity". Biochem. Biophys. Res. Commun. 191 (1): 224–231. doi:10.1006/bbrc.1993.1206. PMID 8447824.
Pelc LA, Chen Z, Gohara DW, et al. (2015). "Why Ser and not Thr brokers catalysis in the trypsin fold". Biochemistry. 54 (7): 1457–64. doi:10.1021/acs.biochem.5b00014. PMC 4342846. PMID 25664608.

ebi.ac.uk

"Clans of Mixed (C, S, T) Catalytic Type". www.ebi.ac.uk. MEROPS. Retrieved 20 Dec 2018.

handle.net

hdl.handle.net

Gulseren G, Khalily MA, Tekinay AB, et al. (2016). "Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis". J. Mater. Chem. B. 4 (26): 4605–4611. doi:10.1039/c6tb00795c. hdl:11693/36666. PMID 32263403.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759. PMID 27378062.

harvard.edu

ui.adsabs.harvard.edu

Buller AR, Townsend CA (2013). "Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad". Proc. Natl. Acad. Sci. U.S.A. 110 (8): E653–61. Bibcode:2013PNAS..110E.653B. doi:10.1073/pnas.1221050110. PMC 3581919. PMID 23382230.
Matthews BW, Sigler PB, Henderson R, et al. (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089): 652–656. Bibcode:1967Natur.214..652M. doi:10.1038/214652a0. PMID 6049071. S2CID 4273406.
Walsh KA, Neurath H (1964). "Trypsinogen and Chymotrypsinogen as Homologous Proteins". Proc. Natl. Acad. Sci. U.S.A. 52 (4): 884–9. Bibcode:1964PNAS...52..884W. doi:10.1073/pnas.52.4.884. PMC 300366. PMID 14224394.
Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 (5178): 337–40. Bibcode:1969Natur.221..337B. doi:10.1038/221337a0. PMID 5764436. S2CID 4214520.
Bazan JF, Fletterick RJ (1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications". Proc. Natl. Acad. Sci. U.S.A. 85 (21): 7872–6. Bibcode:1988PNAS...85.7872B. doi:10.1073/pnas.85.21.7872. PMC 282299. PMID 3186696.
Frey PA, Whitt SA, Tobin JB (1994). "A low-barrier hydrogen bond in the catalytic triad of serine proteases". Science. 264 (5167): 1927–30. Bibcode:1994Sci...264.1927F. doi:10.1126/science.7661899. PMID 7661899.
Ash EL, Sudmeier JL, De Fabo EC, et al. (1997). "A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment". Science. 278 (5340): 1128–32. Bibcode:1997Sci...278.1128A. doi:10.1126/science.278.5340.1128. PMID 9353195.
Agback P, Agback T (2018). "Direct evidence of a low barrier hydrogen bond in the catalytic triad of a Serine protease". Sci. Rep. 8 (1): 10078. Bibcode:2018NatSR...810078A. doi:10.1038/s41598-018-28441-7. PMC 6031666. PMID 29973622.
Warshel A, Papazyan A (1996). "Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13665–70. Bibcode:1996PNAS...9313665W. doi:10.1073/pnas.93.24.13665. PMC 19385. PMID 8942991.
Polgár L, Asbóth B (1986). "The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state". J. Theor. Biol. 121 (3): 323–6. Bibcode:1986JThBi.121..323P. doi:10.1016/s0022-5193(86)80111-4. PMID 3540454.
Damblon C, Raquet X, Lian LY, et al. (1996). "The catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1747–52. Bibcode:1996PNAS...93.1747D. doi:10.1073/pnas.93.5.1747. PMC 39852. PMID 8700829.
Brannigan JA, Dodson G, Duggleby HJ, et al. (1995). "A protein catalytic framework with an N-terminal nucleophile is capable of self-activation". Nature. 378 (6555): 416–9. Bibcode:1995Natur.378..416B. doi:10.1038/378416a0. PMID 7477383. S2CID 4277904.
Cerqueira NM, Moorthy H, Fernandes PA, et al. (2017). "The mechanism of the Ser-(cis)Ser-Lys catalytic triad of peptide amidases". Phys. Chem. Chem. Phys. 19 (19): 12343–12354. Bibcode:2017PCCP...1912343C. doi:10.1039/C7CP00277G. PMID 28453015. Archived from the original on 2017-12-24. Retrieved 2017-12-24.
Jackson DY, Burnier J, Quan C, et al. (1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183): 243–7. Bibcode:1994Sci...266..243J. doi:10.1126/science.7939659. JSTOR 2884761. PMID 7939659.
Nothling MD, Ganesan A, Condic-Jurkic K, et al. (2017). "Simple Design of an Enzyme-Inspired Supported Catalyst Based on a Catalytic Triad". Chem. 2 (5): 732–745. Bibcode:2017Chem....2..732N. doi:10.1016/j.chempr.2017.04.004.
Stehle F, Brandt W, Stubbs MT, et al. (2009). "Sinapoyltransferases in the light of molecular evolution". Phytochemistry. Evolution of Metabolic Diversity. 70 (15–16): 1652–62. Bibcode:2009PChem..70.1652S. doi:10.1016/j.phytochem.2009.07.023. PMID 19695650.
Smith JL, Zaluzec EJ, Wery JP, et al. (1994). "Structure of the allosteric regulatory enzyme of purine biosynthesis". Science. 264 (5164): 1427–33. Bibcode:1994Sci...264.1427S. doi:10.1126/science.8197456. PMID 8197456.

jstor.org

Jackson DY, Burnier J, Quan C, et al. (1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183): 243–7. Bibcode:1994Sci...266..243J. doi:10.1126/science.7939659. JSTOR 2884761. PMID 7939659.

nih.gov

pubmed.ncbi.nlm.nih.gov

Dodson G, Wlodawer A (1998). "Catalytic triads and their relatives". Trends Biochem. Sci. 23 (9): 347–52. doi:10.1016/S0968-0004(98)01254-7. PMID 9787641.
Buller AR, Townsend CA (2013). "Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad". Proc. Natl. Acad. Sci. U.S.A. 110 (8): E653–61. Bibcode:2013PNAS..110E.653B. doi:10.1073/pnas.1221050110. PMC 3581919. PMID 23382230.
Neurath H (1994). "Proteolytic enzymes past and present: the second golden era. Recollections, special section in honor of Max Perutz". Protein Sci. 3 (10): 1734–9. doi:10.1002/pro.5560031013. PMC 2142620. PMID 7849591.
Ohman KP, Hoffman A, Keiser HR (1990). "Endothelin-induced vasoconstriction and release of atrial natriuretic peptides in the rat". Acta Physiol. Scand. 138 (4): 549–56. doi:10.1111/j.1748-1716.1990.tb08883.x. PMID 2141214.
Matthews BW, Sigler PB, Henderson R, et al. (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089): 652–656. Bibcode:1967Natur.214..652M. doi:10.1038/214652a0. PMID 6049071. S2CID 4273406.
Walsh KA, Neurath H (1964). "Trypsinogen and Chymotrypsinogen as Homologous Proteins". Proc. Natl. Acad. Sci. U.S.A. 52 (4): 884–9. Bibcode:1964PNAS...52..884W. doi:10.1073/pnas.52.4.884. PMC 300366. PMID 14224394.
de Haën C, Neurath H, Teller DC (1975). "The phylogeny of trypsin-related serine proteases and their zymogens. New methods for the investigation of distant evolutionary relationships". J. Mol. Biol. 92 (2): 225–59. doi:10.1016/0022-2836(75)90225-9. PMID 1142424.
Lesk AM, Fordham WD (1996). "Conservation and variability in the structures of serine proteinases of the chymotrypsin family". J. Mol. Biol. 258 (3): 501–37. doi:10.1006/jmbi.1996.0264. PMID 8642605.
Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 (5178): 337–40. Bibcode:1969Natur.221..337B. doi:10.1038/221337a0. PMID 5764436. S2CID 4214520.
Gorbalenya AE, Blinov VM, Donchenko AP (1986). "Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families". FEBS Lett. 194 (2): 253–7. doi:10.1016/0014-5793(86)80095-3. PMID 3000829. S2CID 23268152.
Bazan JF, Fletterick RJ (1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications". Proc. Natl. Acad. Sci. U.S.A. 85 (21): 7872–6. Bibcode:1988PNAS...85.7872B. doi:10.1073/pnas.85.21.7872. PMC 282299. PMID 3186696.
Phan J, Zdanov A, Evdokimov AG, et al. (2002). "Structural basis for the substrate specificity of tobacco etch virus protease". J. Biol. Chem. 277 (52): 50564–72. doi:10.1074/jbc.M207224200. PMID 12377789.
Rawlings ND, Barrett AJ (1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. doi:10.1042/bj2900205. PMC 1132403. PMID 8439290.
Rawlings ND, Barrett AJ, Bateman A (2010). "MEROPS: the peptidase database". Nucleic Acids Res. 38 (supl_1): D227–33. doi:10.1093/nar/gkp971. PMC 2808883. PMID 19892822.
Frey PA, Whitt SA, Tobin JB (1994). "A low-barrier hydrogen bond in the catalytic triad of serine proteases". Science. 264 (5167): 1927–30. Bibcode:1994Sci...264.1927F. doi:10.1126/science.7661899. PMID 7661899.
Ash EL, Sudmeier JL, De Fabo EC, et al. (1997). "A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment". Science. 278 (5340): 1128–32. Bibcode:1997Sci...278.1128A. doi:10.1126/science.278.5340.1128. PMID 9353195.
Agback P, Agback T (2018). "Direct evidence of a low barrier hydrogen bond in the catalytic triad of a Serine protease". Sci. Rep. 8 (1): 10078. Bibcode:2018NatSR...810078A. doi:10.1038/s41598-018-28441-7. PMC 6031666. PMID 29973622.
Schutz CN, Warshel A (2004). "The low barrier hydrogen bond (LBHB) proposal revisited: the case of the Asp... His pair in serine proteases". Proteins. 55 (3): 711–23. doi:10.1002/prot.20096. PMID 15103633. S2CID 34229297.
Warshel A, Papazyan A (1996). "Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13665–70. Bibcode:1996PNAS...9313665W. doi:10.1073/pnas.93.24.13665. PMC 19385. PMID 8942991.
Fersht, A.R.; Requena, Y (1971). "Mechanism of the Chymotrypsin-Catalyzed Hydrolysis of Amides. pH Dependence of kc and Km.' Kinetic Detection of an Intermediate". J. Am. Chem. Soc. 93 (25): 7079–87. doi:10.1021/ja00754a066. PMID 5133099.
Zeeberg, B; Caswell, M; Caplow, M (1973). "Concerning a reported change in rate-determining step in chymotrypsin catalysis". J. Am. Chem. Soc. 95 (8): 2734–5. doi:10.1021/ja00789a081. PMID 4694533.
Ekici OD, Paetzel M, Dalbey RE (2008). "Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration". Protein Sci. 17 (12): 2023–37. doi:10.1110/ps.035436.108. PMC 2590910. PMID 18824507.
McGrath ME, Wilke ME, Higaki JN, et al. (1989). "Crystal structures of two engineered thiol trypsins". Biochemistry. 28 (24): 9264–70. doi:10.1021/bi00450a005. PMID 2611228.
Polgár L, Asbóth B (1986). "The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state". J. Theor. Biol. 121 (3): 323–6. Bibcode:1986JThBi.121..323P. doi:10.1016/s0022-5193(86)80111-4. PMID 3540454.
Brandt W, Wessjohann LA (2005). "The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state". ChemBioChem. 6 (2): 386–94. doi:10.1002/cbic.200400276. PMID 15651042. S2CID 25575160.
Damblon C, Raquet X, Lian LY, et al. (1996). "The catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1747–52. Bibcode:1996PNAS...93.1747D. doi:10.1073/pnas.93.5.1747. PMC 39852. PMID 8700829.
Jelsch C, Lenfant F, Masson JM, et al. (1992). "Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution". FEBS Lett. 299 (2): 135–42. doi:10.1016/0014-5793(92)80232-6. PMID 1544485.
Brannigan JA, Dodson G, Duggleby HJ, et al. (1995). "A protein catalytic framework with an N-terminal nucleophile is capable of self-activation". Nature. 378 (6555): 416–9. Bibcode:1995Natur.378..416B. doi:10.1038/378416a0. PMID 7477383. S2CID 4277904.
Cheng H, Grishin NV (2005). "DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain". Protein Sci. 14 (7): 1902–10. doi:10.1110/ps.051364905. PMC 2253344. PMID 15937278.
Sun Y, Yin S, Feng Y, et al. (2014). "Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad". J. Biol. Chem. 289 (22): 15867–79. doi:10.1074/jbc.m113.535641. PMC 4140940. PMID 24737327.
Rauwerdink A, Kazlauskas RJ (2015). "How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes". ACS Catal. 5 (10): 6153–6176. doi:10.1021/acscatal.5b01539. PMC 5455348. PMID 28580193.
Beveridge AJ (1996). "A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinases". Protein Sci. 5 (7): 1355–65. doi:10.1002/pro.5560050714. PMC 2143470. PMID 8819168.
Allen MD, Buchberger A, Bycroft M (2006). "The PUB domain functions as a p97 binding module in human peptide N-glycanase". J. Biol. Chem. 281 (35): 25502–8. doi:10.1074/jbc.M601173200. PMID 16807242.
Sanchez-Pulido L, Ponting CP (2016). "Vasohibins: new transglutaminase-like cysteine proteases possessing a non-canonical Cys-His-Ser catalytic triad". Bioinformatics. 32 (10): 1441–5. doi:10.1093/bioinformatics/btv761. PMC 4866520. PMID 26794318.
Sato Y, Sonoda H (2007). "The vasohibin family: a negative regulatory system of angiogenesis genetically programmed in endothelial cells". Arterioscler. Thromb. Vasc. Biol. 27 (1): 37–41. doi:10.1161/01.atv.0000252062.48280.61. PMID 17095714.
Shin S, Yun YS, Koo HM, et al. (2003). "Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad". J. Biol. Chem. 278 (27): 24937–43. doi:10.1074/jbc.M302156200. PMID 12711609.
Cerqueira NM, Moorthy H, Fernandes PA, et al. (2017). "The mechanism of the Ser-(cis)Ser-Lys catalytic triad of peptide amidases". Phys. Chem. Chem. Phys. 19 (19): 12343–12354. Bibcode:2017PCCP...1912343C. doi:10.1039/C7CP00277G. PMID 28453015. Archived from the original on 2017-12-24. Retrieved 2017-12-24.
Toscano MD, Woycechowsky KJ, Hilvert D (2007). "Minimalist active-site redesign: teaching old enzymes new tricks". Angew. Chem. 46 (18): 3212–36. doi:10.1002/anie.200604205. PMID 17450624.
Abrahmsén L, Tom J, Burnier J, et al. (1991). "Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution". Biochemistry. 30 (17): 4151–9. CiteSeerX 10.1.1.461.9606. doi:10.1021/bi00231a007. PMID 2021606.
Jackson DY, Burnier J, Quan C, et al. (1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183): 243–7. Bibcode:1994Sci...266..243J. doi:10.1126/science.7939659. JSTOR 2884761. PMID 7939659.
Syed R, Wu ZP, Hogle JM, et al. (1993). "Crystal structure of selenosubtilisin at 2.0-A resolution". Biochemistry. 32 (24): 6157–64. doi:10.1021/bi00075a007. PMID 8512925.
Mao S, Dong Z, Liu J, et al. (2005). "Semisynthetic tellurosubtilisin with glutathione peroxidase activity". J. Am. Chem. Soc. 127 (33): 11588–9. doi:10.1021/ja052451v. PMID 16104720.
Shafee T, Gatti-Lafranconi P, Minter R, et al. (2015). "Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease". ChemBioChem. 16 (13): 1866–9. doi:10.1002/cbic.201500295. PMC 4576821. PMID 26097079.
Okochi N, Kato-Murai M, Kadonosono T, et al. (2007). "Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface". Appl. Microbiol. Biotechnol. 77 (3): 597–603. doi:10.1007/s00253-007-1197-0. PMID 17899065. S2CID 35590920.
Rajagopalan S, Wang C, Yu K, et al. (2014). "Design of activated serine-containing catalytic triads with atomic-level accuracy". Nat. Chem. Biol. 10 (5): 386–91. doi:10.1038/nchembio.1498. PMC 4048123. PMID 24705591.
Bhowmick D, Mugesh G (2015). "Introduction of a catalytic triad increases the glutathione peroxidase-like activity of diaryl diselenides". Org. Biomol. Chem. 13 (34): 9072–82. doi:10.1039/C5OB01294E. PMID 26220806.
Bhowmick D, Mugesh G (2015). "Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics". Org. Biomol. Chem. 13 (41): 10262–72. doi:10.1039/c5ob01665g. PMID 26372527.
Gulseren G, Khalily MA, Tekinay AB, et al. (2016). "Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis". J. Mater. Chem. B. 4 (26): 4605–4611. doi:10.1039/c6tb00795c. hdl:11693/36666. PMID 32263403.
Halabi N, Rivoire O, Leibler S, et al. (2009). "Protein sectors: evolutionary units of three-dimensional structure". Cell. 138 (4): 774–86. doi:10.1016/j.cell.2009.07.038. PMC 3210731. PMID 19703402.
Murzin AG (1998). "How far divergent evolution goes in proteins". Current Opinion in Structural Biology. 8 (3): 380–387. doi:10.1016/S0959-440X(98)80073-0. PMID 9666335.
Gerlt JA, Babbitt PC (2001). "Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies". Annu. Rev. Biochem. 70 (1): 209–46. doi:10.1146/annurev.biochem.70.1.209. PMID 11395407.
Murphy JM, Farhan H, Eyers PA (2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochem. Soc. Trans. 45 (2): 537–544. doi:10.1042/bst20160400. PMID 28408493.
Stehle F, Brandt W, Stubbs MT, et al. (2009). "Sinapoyltransferases in the light of molecular evolution". Phytochemistry. Evolution of Metabolic Diversity. 70 (15–16): 1652–62. Bibcode:2009PChem..70.1652S. doi:10.1016/j.phytochem.2009.07.023. PMID 19695650.
Dimitriou PS, Denesyuk A, Takahashi S, et al. (2017). "Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families". Proteins. 85 (10): 1845–1855. doi:10.1002/prot.25338. PMID 28643343. S2CID 25363240.
Smith JL (1998). "Glutamine PRPP amidotransferase: snapshots of an enzyme in action". Current Opinion in Structural Biology. 8 (6): 686–94. doi:10.1016/s0959-440x(98)80087-0. PMID 9914248.
Smith JL, Zaluzec EJ, Wery JP, et al. (1994). "Structure of the allosteric regulatory enzyme of purine biosynthesis". Science. 264 (5164): 1427–33. Bibcode:1994Sci...264.1427S. doi:10.1126/science.8197456. PMID 8197456.
Fischer K, Reynolds SL (2015). "Pseudoproteases: mechanisms and function". Biochem. J. 468 (1): 17–24. doi:10.1042/BJ20141506. PMID 25940733.
Todd AE, Orengo CA, Thornton JM (2002). "Sequence and structural differences between enzyme and nonenzyme homologs". Structure. 10 (10): 1435–51. doi:10.1016/s0969-2126(02)00861-4. PMID 12377129.
Iversen LF, Kastrup JS, Bjørn SE, et al. (1997). "Structure of HBP, a multifunctional protein with a serine proteinase fold". Nat. Struct. Biol. 4 (4): 265–8. doi:10.1038/nsb0497-265. PMID 9095193. S2CID 19949043.
Zettl M, Adrain C, Strisovsky K, et al. (2011). "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling". Cell. 145 (1): 79–91. doi:10.1016/j.cell.2011.02.047. PMC 3149277. PMID 21439629.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759. PMID 27378062.
Cheng CY, Morris I, Bardin CW (1993). "Testins Are Structurally Related to the Mouse Cysteine Proteinase Precursor But Devoid of Any Protease/Anti-Protease Activity". Biochem. Biophys. Res. Commun. 191 (1): 224–231. doi:10.1006/bbrc.1993.1206. PMID 8447824.
Pelc LA, Chen Z, Gohara DW, et al. (2015). "Why Ser and not Thr brokers catalysis in the trypsin fold". Biochemistry. 54 (7): 1457–64. doi:10.1021/acs.biochem.5b00014. PMC 4342846. PMID 25664608.

ncbi.nlm.nih.gov

Buller AR, Townsend CA (2013). "Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad". Proc. Natl. Acad. Sci. U.S.A. 110 (8): E653–61. Bibcode:2013PNAS..110E.653B. doi:10.1073/pnas.1221050110. PMC 3581919. PMID 23382230.
Stryer L, Berg JM, Tymoczko JL (2002). "9 Catalytic Strategies". Biochemistry (5th ed.). San Francisco: W.H. Freeman. ISBN 9780716749554.
Neurath H (1994). "Proteolytic enzymes past and present: the second golden era. Recollections, special section in honor of Max Perutz". Protein Sci. 3 (10): 1734–9. doi:10.1002/pro.5560031013. PMC 2142620. PMID 7849591.
Walsh KA, Neurath H (1964). "Trypsinogen and Chymotrypsinogen as Homologous Proteins". Proc. Natl. Acad. Sci. U.S.A. 52 (4): 884–9. Bibcode:1964PNAS...52..884W. doi:10.1073/pnas.52.4.884. PMC 300366. PMID 14224394.
Bazan JF, Fletterick RJ (1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications". Proc. Natl. Acad. Sci. U.S.A. 85 (21): 7872–6. Bibcode:1988PNAS...85.7872B. doi:10.1073/pnas.85.21.7872. PMC 282299. PMID 3186696.
Rawlings ND, Barrett AJ (1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. doi:10.1042/bj2900205. PMC 1132403. PMID 8439290.
Rawlings ND, Barrett AJ, Bateman A (2010). "MEROPS: the peptidase database". Nucleic Acids Res. 38 (supl_1): D227–33. doi:10.1093/nar/gkp971. PMC 2808883. PMID 19892822.
Agback P, Agback T (2018). "Direct evidence of a low barrier hydrogen bond in the catalytic triad of a Serine protease". Sci. Rep. 8 (1): 10078. Bibcode:2018NatSR...810078A. doi:10.1038/s41598-018-28441-7. PMC 6031666. PMID 29973622.
Warshel A, Papazyan A (1996). "Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13665–70. Bibcode:1996PNAS...9313665W. doi:10.1073/pnas.93.24.13665. PMC 19385. PMID 8942991.
Ekici OD, Paetzel M, Dalbey RE (2008). "Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration". Protein Sci. 17 (12): 2023–37. doi:10.1110/ps.035436.108. PMC 2590910. PMID 18824507.
Damblon C, Raquet X, Lian LY, et al. (1996). "The catalytic mechanism of beta-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1747–52. Bibcode:1996PNAS...93.1747D. doi:10.1073/pnas.93.5.1747. PMC 39852. PMID 8700829.
Cheng H, Grishin NV (2005). "DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain". Protein Sci. 14 (7): 1902–10. doi:10.1110/ps.051364905. PMC 2253344. PMID 15937278.
Sun Y, Yin S, Feng Y, et al. (2014). "Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad". J. Biol. Chem. 289 (22): 15867–79. doi:10.1074/jbc.m113.535641. PMC 4140940. PMID 24737327.
Rauwerdink A, Kazlauskas RJ (2015). "How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes". ACS Catal. 5 (10): 6153–6176. doi:10.1021/acscatal.5b01539. PMC 5455348. PMID 28580193.
Beveridge AJ (1996). "A theoretical study of the active sites of papain and S195C rat trypsin: implications for the low reactivity of mutant serine proteinases". Protein Sci. 5 (7): 1355–65. doi:10.1002/pro.5560050714. PMC 2143470. PMID 8819168.
Sanchez-Pulido L, Ponting CP (2016). "Vasohibins: new transglutaminase-like cysteine proteases possessing a non-canonical Cys-His-Ser catalytic triad". Bioinformatics. 32 (10): 1441–5. doi:10.1093/bioinformatics/btv761. PMC 4866520. PMID 26794318.
Shafee T, Gatti-Lafranconi P, Minter R, et al. (2015). "Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease". ChemBioChem. 16 (13): 1866–9. doi:10.1002/cbic.201500295. PMC 4576821. PMID 26097079.
Rajagopalan S, Wang C, Yu K, et al. (2014). "Design of activated serine-containing catalytic triads with atomic-level accuracy". Nat. Chem. Biol. 10 (5): 386–91. doi:10.1038/nchembio.1498. PMC 4048123. PMID 24705591.
Halabi N, Rivoire O, Leibler S, et al. (2009). "Protein sectors: evolutionary units of three-dimensional structure". Cell. 138 (4): 774–86. doi:10.1016/j.cell.2009.07.038. PMC 3210731. PMID 19703402.
Zettl M, Adrain C, Strisovsky K, et al. (2011). "Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling". Cell. 145 (1): 79–91. doi:10.1016/j.cell.2011.02.047. PMC 3149277. PMID 21439629.
Pelc LA, Chen Z, Gohara DW, et al. (2015). "Why Ser and not Thr brokers catalysis in the trypsin fold". Biochemistry. 54 (7): 1457–64. doi:10.1021/acs.biochem.5b00014. PMC 4342846. PMID 25664608.

psu.edu

citeseerx.ist.psu.edu

Abrahmsén L, Tom J, Burnier J, et al. (1991). "Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution". Biochemistry. 30 (17): 4151–9. CiteSeerX 10.1.1.461.9606. doi:10.1021/bi00231a007. PMID 2021606.

rsc.org

pubs.rsc.org

Cerqueira NM, Moorthy H, Fernandes PA, et al. (2017). "The mechanism of the Ser-(cis)Ser-Lys catalytic triad of peptide amidases". Phys. Chem. Chem. Phys. 19 (19): 12343–12354. Bibcode:2017PCCP...1912343C. doi:10.1039/C7CP00277G. PMID 28453015. Archived from the original on 2017-12-24. Retrieved 2017-12-24.

sanger.ac.uk

merops.sanger.ac.uk

TEV protease MEROPS: clan PA, family C4
Cytomegalovirus protease MEROPS: clan SH, family S21
Chymotrypsin MEROPS: clan PA, family S1
Papain MEROPS: clan CA, family C1
Sedolisin protease MEROPS: clan SB, family 53
Vasohibin protease MEROPS: clan CA
Proteasome MEROPS: clan PB, family T1
Ornithine acyltransferases MEROPS: clan PE, family T5
Penicillin acylase G MEROPS: clan PB, family S45
Penicillin acylase V MEROPS: clan PB, family C59
amidophosphoribosyltransferase MEROPS: clan PB, family C44
Subtilisin MEROPS: clan SB, family S8
Prolyl oligopeptidase MEROPS: clan SC, family S9

semanticscholar.org

api.semanticscholar.org

Matthews BW, Sigler PB, Henderson R, et al. (1967). "Three-dimensional structure of tosyl-α-chymotrypsin". Nature. 214 (5089): 652–656. Bibcode:1967Natur.214..652M. doi:10.1038/214652a0. PMID 6049071. S2CID 4273406.
Blow DM, Birktoft JJ, Hartley BS (1969). "Role of a buried acid group in the mechanism of action of chymotrypsin". Nature. 221 (5178): 337–40. Bibcode:1969Natur.221..337B. doi:10.1038/221337a0. PMID 5764436. S2CID 4214520.
Gorbalenya AE, Blinov VM, Donchenko AP (1986). "Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families". FEBS Lett. 194 (2): 253–7. doi:10.1016/0014-5793(86)80095-3. PMID 3000829. S2CID 23268152.
Schutz CN, Warshel A (2004). "The low barrier hydrogen bond (LBHB) proposal revisited: the case of the Asp... His pair in serine proteases". Proteins. 55 (3): 711–23. doi:10.1002/prot.20096. PMID 15103633. S2CID 34229297.
Brandt W, Wessjohann LA (2005). "The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state". ChemBioChem. 6 (2): 386–94. doi:10.1002/cbic.200400276. PMID 15651042. S2CID 25575160.
Brannigan JA, Dodson G, Duggleby HJ, et al. (1995). "A protein catalytic framework with an N-terminal nucleophile is capable of self-activation". Nature. 378 (6555): 416–9. Bibcode:1995Natur.378..416B. doi:10.1038/378416a0. PMID 7477383. S2CID 4277904.
Okochi N, Kato-Murai M, Kadonosono T, et al. (2007). "Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface". Appl. Microbiol. Biotechnol. 77 (3): 597–603. doi:10.1007/s00253-007-1197-0. PMID 17899065. S2CID 35590920.
Dimitriou PS, Denesyuk A, Takahashi S, et al. (2017). "Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families". Proteins. 85 (10): 1845–1855. doi:10.1002/prot.25338. PMID 28643343. S2CID 25363240.
Iversen LF, Kastrup JS, Bjørn SE, et al. (1997). "Structure of HBP, a multifunctional protein with a serine proteinase fold". Nat. Struct. Biol. 4 (4): 265–8. doi:10.1038/nsb0497-265. PMID 9095193. S2CID 19949043.

web.archive.org

Cerqueira NM, Moorthy H, Fernandes PA, et al. (2017). "The mechanism of the Ser-(cis)Ser-Lys catalytic triad of peptide amidases". Phys. Chem. Chem. Phys. 19 (19): 12343–12354. Bibcode:2017PCCP...1912343C. doi:10.1039/C7CP00277G. PMID 28453015. Archived from the original on 2017-12-24. Retrieved 2017-12-24.

worldcat.org

search.worldcat.org

Devillanova FA, Du Mont WW (2013). Handbook of Chalcogen Chemistry. Vol. 1: new perspectives in sulfur, selenium and tellurium (2nd ed.). Cambridge: RSC. ISBN 9781849736237. OCLC 868953797.