Tríade catalítica (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "Tríade catalítica" in Galician language version.

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67doi.org

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14sanger.ac.uk

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1ebi.ac.uk

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archive.org

Dodson G, Wlodawer A (1998). "Catalytic triads and their relatives". Trends Biochem. Sci. 23 (9): 347–52. PMID 9787641. doi:10.1016/S0968-0004(98)01254-7.
Perutz, Max (1992). Protein structure. New approaches to disease and therapy. New York: W.H. Freeman and Co. ISBN 9780716770213.
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. PMID 6049071. doi:10.1038/214652a0.
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. PMID 5764436. doi:10.1038/221337a0.
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. PMID 3000829. doi:10.1016/0014-5793(86)80095-3.
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. PMID 7661899. doi:10.1126/science.7661899.
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. PMID 1544485. doi:10.1016/0014-5793(92)80232-6.
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. PMID 16807242. doi:10.1074/jbc.M601173200.
Sato Y, Sonoda H (2007). "The vasohibin family: a negative regulatory system of angiogenesis genetically programmed in endothelial cells". Arter. Thromb. Vasc. Biol. 27 (1): 37–41. PMID 17095714. doi:10.1161/01.atv.0000252062.48280.61.
Bouroushian, Mirtat (2010). "Electrochemistry of the Chalcogens". Electrochemistry of Metal Chalcogenides. Monographs in Electrochemistry. Berlin, Heidelberg: Springer. pp. 57–75. ISBN 9783642039669. doi:10.1007/978-3-642-03967-6_2.
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. PMID 8197456. doi:10.1126/science.8197456.

cam.ac.uk

repository.cam.ac.uk

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

doi.org

dx.doi.org

Dodson G, Wlodawer A (1998). "Catalytic triads and their relatives". Trends Biochem. Sci. 23 (9): 347–52. PMID 9787641. doi:10.1016/S0968-0004(98)01254-7.
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. PMC 3581919. PMID 23382230. doi:10.1073/pnas.1221050110.
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. PMC 2142620. PMID 7849591. doi:10.1002/pro.5560031013.
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. PMID 2141214. doi:10.1111/j.1748-1716.1990.tb08883.x.
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. PMID 6049071. doi:10.1038/214652a0.
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. PMC 300366. PMID 1422439. doi:10.1073/pnas.52.4.884.
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. PMID 1142424. doi:10.1016/0022-2836(75)90225-9.
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. PMID 8642605. doi:10.1006/jmbi.1996.0264.
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. PMID 5764436. doi:10.1038/221337a0.
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. PMID 3000829. doi:10.1016/0014-5793(86)80095-3.
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. PMC 282299. PMID 3186696. doi:10.1073/pnas.85.21.7872.
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. PMID 12377789. doi:10.1074/jbc.M207224200.
Rawlings ND, Barrett AJ (1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. PMC 1132403. PMID 8439290. doi:10.1042/bj2900205.
Rawlings ND, Barrett AJ, Bateman A (2010). "MEROPS: the peptidase database". Nucleic Acids Res. 38 (supl_1): D227–33. PMC 2808883. PMID 19892822. doi:10.1093/nar/gkp971.
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. PMID 7661899. doi:10.1126/science.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. PMID 9353195. doi:10.1126/science.278.5340.1128.
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. PMC 6031666. PMID 29973622. doi:10.1038/s41598-018-28441-7.
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. PMID 15103633. doi:10.1002/prot.20096.
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. PMC 19385. PMID 8942991. doi:10.1073/pnas.93.24.13665.
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. PMID 5133099. doi:10.1021/ja00754a066.
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. PMID 4694533. doi:10.1021/ja00789a081.
Shafee, Thomas (2014). Evolvability of a viral protease: experimental evolution of catalysis, robustness and specificity (Tese). 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. PMC 2590910. PMID 18824507. doi:10.1110/ps.035436.108.
McGrath ME, Wilke ME, Higaki JN, et al. (1989). "Crystal structures of two engineered thiol trypsins". Biochemistry 28 (24): 9264–70. PMID 2611228. doi:10.1021/bi00450a005.
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. PMID 3540454. doi:10.1016/s0022-5193(86)80111-4.
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. PMID 15651042. doi:10.1002/cbic.200400276.
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. PMC 39852. PMID 8700829. doi:10.1073/pnas.93.5.1747.
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. PMID 1544485. doi:10.1016/0014-5793(92)80232-6.
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. PMID 7477383. doi:10.1038/378416a0.
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. PMC 2253344. PMID 15937278. doi:10.1110/ps.051364905.
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. PMC 4140940. PMID 24737327. doi:10.1074/jbc.m113.535641.
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. PMC 5455348. PMID 28580193. doi:10.1021/acscatal.5b01539.
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. PMC 2143470. PMID 8819168. doi:10.1002/pro.5560050714.
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. PMID 16807242. doi:10.1074/jbc.M601173200.
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. PMC 4866520. PMID 26794318. doi:10.1093/bioinformatics/btv761.
Sato Y, Sonoda H (2007). "The vasohibin family: a negative regulatory system of angiogenesis genetically programmed in endothelial cells". Arter. Thromb. Vasc. Biol. 27 (1): 37–41. PMID 17095714. doi:10.1161/01.atv.0000252062.48280.61.
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. PMID 12711609. doi:10.1074/jbc.M302156200.
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. PMID 28453015. doi:10.1039/C7CP00277G. Arquivado dende o orixinal o 24 de decembro de 2017. Consultado o 25 de agosto de 2021.
Toscano MD, Woycechowsky KJ, Hilvert D (2007). "Minimalist active-site redesign: teaching old enzymes new tricks". Angew. Chem. 46 (18): 3212–36. PMID 17450624. doi:10.1002/anie.200604205.
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. PMID 17899065. doi:10.1007/s00253-007-1197-0.
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. doi:10.1016/j.chempr.2017.04.004.
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. PMID 2021606. doi:10.1021/bi00231a007.
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. JSTOR 2884761. PMID 7939659. doi:10.1126/science.7939659.
Syed R, Wu ZP, Hogle JM, et al. (1993). "Crystal structure of selenosubtilisin at 2.0-A resolution". Biochemistry 32 (24): 6157–64. PMID 8512925. doi:10.1021/bi00075a007.
Mao S, Dong Z, Liu J, et al. (2005). "Semisynthetic tellurosubtilisin with glutathione peroxidase activity". J. Am. Chem. Soc. 127 (33): 11588–9. PMID 16104720. doi:10.1021/ja052451v.
Bouroushian, Mirtat (2010). "Electrochemistry of the Chalcogens". Electrochemistry of Metal Chalcogenides. Monographs in Electrochemistry. Berlin, Heidelberg: Springer. pp. 57–75. ISBN 9783642039669. doi:10.1007/978-3-642-03967-6_2.
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. PMC 4576821. PMID 26097079. doi:10.1002/cbic.201500295.
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. PMC 4048123. PMID 24705591. doi:10.1038/nchembio.1498.
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. PMID 26220806. doi:10.1039/C5OB01294E.
Bhowmick D, Mugesh G (2015). "Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics". Org. Biomol. Chem. 13 (41): 10262–72. PMID 26372527. doi:10.1039/c5ob01665g.
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. PMID 32263403. doi:10.1039/c6tb00795c. hdl:11693/36666.
Halabi N, Rivoire O, Leibler S, et al. (2009). "Protein sectors: evolutionary units of three-dimensional structure". Cell 138 (4): 774–86. PMC 3210731. PMID 19703402. doi:10.1016/j.cell.2009.07.038.
Murzin AG (1998). "How far divergent evolution goes in proteins". Current Opinion in Structural Biology 8 (3): 380–387. PMID 9666335. doi:10.1016/S0959-440X(98)80073-0.
Gerlt JA, Babbitt PC (2001). "Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies". Annu. Rev. Biochem. 70 (1): 209–46. PMID 11395407. doi:10.1146/annurev.biochem.70.1.209.
Murphy JM, Farhan H, Eyers PA (2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochem. Soc. Trans. 45 (2): 537–544. PMID 28408493. doi:10.1042/bst20160400.
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. PMID 19695650. doi:10.1016/j.phytochem.2009.07.023.
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. PMID 28643343. doi:10.1002/prot.25338.
Smith JL (1998). "Glutamine PRPP amidotransferase: snapshots of an enzyme in action". Current Opinion in Structural Biology 8 (6): 686–94. PMID 9914248. doi:10.1016/s0959-440x(98)80087-0.
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. PMID 8197456. doi:10.1126/science.8197456.
Fischer K, Reynolds SL (2015). "Pseudoproteases: mechanisms and function". Biochem. J. 468 (1): 17–24. PMID 25940733. doi:10.1042/BJ20141506.
Todd AE, Orengo CA, Thornton JM (2002). "Sequence and structural differences between enzyme and nonenzyme homologs". Structure 10 (10): 1435–51. PMID 12377129. doi:10.1016/s0969-2126(02)00861-4.
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. PMID 9095193. doi:10.1038/nsb0497-265.
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. PMC 3149277. PMID 21439629. doi:10.1016/j.cell.2011.02.047.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. PMID 27378062. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759.
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. PMID 8447824. doi:10.1006/bbrc.1993.1206.
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. PMC 4342846. PMID 25664608. doi:10.1021/acs.biochem.5b00014.

ebi.ac.uk

"Clans of Mixed (C, S, T) Catalytic Type". www.ebi.ac.uk. MEROPS. Consultado o 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. PMID 32263403. doi:10.1039/c6tb00795c. hdl:11693/36666.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. PMID 27378062. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759.

harvard.edu

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. PMC 3581919. PMID 23382230. doi:10.1073/pnas.1221050110.
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. PMID 6049071. doi:10.1038/214652a0.
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. PMC 300366. PMID 1422439. doi:10.1073/pnas.52.4.884.
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. PMID 5764436. doi:10.1038/221337a0.
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. PMC 282299. PMID 3186696. doi:10.1073/pnas.85.21.7872.
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. PMID 7661899. doi:10.1126/science.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. PMID 9353195. doi:10.1126/science.278.5340.1128.
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. PMC 6031666. PMID 29973622. doi:10.1038/s41598-018-28441-7.
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. PMC 19385. PMID 8942991. doi:10.1073/pnas.93.24.13665.
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. PMID 3540454. doi:10.1016/s0022-5193(86)80111-4.
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. PMC 39852. PMID 8700829. doi:10.1073/pnas.93.5.1747.
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. PMID 7477383. doi:10.1038/378416a0.
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. PMID 28453015. doi:10.1039/C7CP00277G. Arquivado dende o orixinal o 24 de decembro de 2017. Consultado o 25 de agosto de 2021.
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. JSTOR 2884761. PMID 7939659. doi:10.1126/science.7939659.
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. PMID 8197456. doi:10.1126/science.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. JSTOR 2884761. PMID 7939659. doi:10.1126/science.7939659.

nih.gov

ncbi.nlm.nih.gov

Dodson G, Wlodawer A (1998). "Catalytic triads and their relatives". Trends Biochem. Sci. 23 (9): 347–52. PMID 9787641. doi:10.1016/S0968-0004(98)01254-7.
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. PMC 3581919. PMID 23382230. doi:10.1073/pnas.1221050110.
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. PMC 2142620. PMID 7849591. doi:10.1002/pro.5560031013.
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. PMID 2141214. doi:10.1111/j.1748-1716.1990.tb08883.x.
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. PMID 6049071. doi:10.1038/214652a0.
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. PMC 300366. PMID 1422439. doi:10.1073/pnas.52.4.884.
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. PMID 1142424. doi:10.1016/0022-2836(75)90225-9.
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. PMID 8642605. doi:10.1006/jmbi.1996.0264.
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. PMID 5764436. doi:10.1038/221337a0.
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. PMID 3000829. doi:10.1016/0014-5793(86)80095-3.
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. PMC 282299. PMID 3186696. doi:10.1073/pnas.85.21.7872.
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. PMID 12377789. doi:10.1074/jbc.M207224200.
Rawlings ND, Barrett AJ (1993). "Evolutionary families of peptidases". Biochem. J. 290 (1): 205–18. PMC 1132403. PMID 8439290. doi:10.1042/bj2900205.
Rawlings ND, Barrett AJ, Bateman A (2010). "MEROPS: the peptidase database". Nucleic Acids Res. 38 (supl_1): D227–33. PMC 2808883. PMID 19892822. doi:10.1093/nar/gkp971.
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. PMID 7661899. doi:10.1126/science.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. PMID 9353195. doi:10.1126/science.278.5340.1128.
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. PMC 6031666. PMID 29973622. doi:10.1038/s41598-018-28441-7.
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. PMID 15103633. doi:10.1002/prot.20096.
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. PMC 19385. PMID 8942991. doi:10.1073/pnas.93.24.13665.
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. PMID 5133099. doi:10.1021/ja00754a066.
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. PMID 4694533. doi:10.1021/ja00789a081.
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. PMC 2590910. PMID 18824507. doi:10.1110/ps.035436.108.
McGrath ME, Wilke ME, Higaki JN, et al. (1989). "Crystal structures of two engineered thiol trypsins". Biochemistry 28 (24): 9264–70. PMID 2611228. doi:10.1021/bi00450a005.
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. PMID 3540454. doi:10.1016/s0022-5193(86)80111-4.
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. PMID 15651042. doi:10.1002/cbic.200400276.
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. PMC 39852. PMID 8700829. doi:10.1073/pnas.93.5.1747.
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. PMID 1544485. doi:10.1016/0014-5793(92)80232-6.
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. PMID 7477383. doi:10.1038/378416a0.
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. PMC 2253344. PMID 15937278. doi:10.1110/ps.051364905.
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. PMC 4140940. PMID 24737327. doi:10.1074/jbc.m113.535641.
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. PMC 5455348. PMID 28580193. doi:10.1021/acscatal.5b01539.
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. PMC 2143470. PMID 8819168. doi:10.1002/pro.5560050714.
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. PMID 16807242. doi:10.1074/jbc.M601173200.
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. PMC 4866520. PMID 26794318. doi:10.1093/bioinformatics/btv761.
Sato Y, Sonoda H (2007). "The vasohibin family: a negative regulatory system of angiogenesis genetically programmed in endothelial cells". Arter. Thromb. Vasc. Biol. 27 (1): 37–41. PMID 17095714. doi:10.1161/01.atv.0000252062.48280.61.
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. PMID 12711609. doi:10.1074/jbc.M302156200.
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. PMID 28453015. doi:10.1039/C7CP00277G. Arquivado dende o orixinal o 24 de decembro de 2017. Consultado o 25 de agosto de 2021.
Toscano MD, Woycechowsky KJ, Hilvert D (2007). "Minimalist active-site redesign: teaching old enzymes new tricks". Angew. Chem. 46 (18): 3212–36. PMID 17450624. doi:10.1002/anie.200604205.
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. PMID 17899065. doi:10.1007/s00253-007-1197-0.
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. PMID 2021606. doi:10.1021/bi00231a007.
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. JSTOR 2884761. PMID 7939659. doi:10.1126/science.7939659.
Syed R, Wu ZP, Hogle JM, et al. (1993). "Crystal structure of selenosubtilisin at 2.0-A resolution". Biochemistry 32 (24): 6157–64. PMID 8512925. doi:10.1021/bi00075a007.
Mao S, Dong Z, Liu J, et al. (2005). "Semisynthetic tellurosubtilisin with glutathione peroxidase activity". J. Am. Chem. Soc. 127 (33): 11588–9. PMID 16104720. doi:10.1021/ja052451v.
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. PMC 4576821. PMID 26097079. doi:10.1002/cbic.201500295.
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. PMC 4048123. PMID 24705591. doi:10.1038/nchembio.1498.
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. PMID 26220806. doi:10.1039/C5OB01294E.
Bhowmick D, Mugesh G (2015). "Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics". Org. Biomol. Chem. 13 (41): 10262–72. PMID 26372527. doi:10.1039/c5ob01665g.
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. PMID 32263403. doi:10.1039/c6tb00795c. hdl:11693/36666.
Halabi N, Rivoire O, Leibler S, et al. (2009). "Protein sectors: evolutionary units of three-dimensional structure". Cell 138 (4): 774–86. PMC 3210731. PMID 19703402. doi:10.1016/j.cell.2009.07.038.
Murzin AG (1998). "How far divergent evolution goes in proteins". Current Opinion in Structural Biology 8 (3): 380–387. PMID 9666335. doi:10.1016/S0959-440X(98)80073-0.
Gerlt JA, Babbitt PC (2001). "Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies". Annu. Rev. Biochem. 70 (1): 209–46. PMID 11395407. doi:10.1146/annurev.biochem.70.1.209.
Murphy JM, Farhan H, Eyers PA (2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochem. Soc. Trans. 45 (2): 537–544. PMID 28408493. doi:10.1042/bst20160400.
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. PMID 19695650. doi:10.1016/j.phytochem.2009.07.023.
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. PMID 28643343. doi:10.1002/prot.25338.
Smith JL (1998). "Glutamine PRPP amidotransferase: snapshots of an enzyme in action". Current Opinion in Structural Biology 8 (6): 686–94. PMID 9914248. doi:10.1016/s0959-440x(98)80087-0.
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. PMID 8197456. doi:10.1126/science.8197456.
Fischer K, Reynolds SL (2015). "Pseudoproteases: mechanisms and function". Biochem. J. 468 (1): 17–24. PMID 25940733. doi:10.1042/BJ20141506.
Todd AE, Orengo CA, Thornton JM (2002). "Sequence and structural differences between enzyme and nonenzyme homologs". Structure 10 (10): 1435–51. PMID 12377129. doi:10.1016/s0969-2126(02)00861-4.
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. PMID 9095193. doi:10.1038/nsb0497-265.
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. PMC 3149277. PMID 21439629. doi:10.1016/j.cell.2011.02.047.
Lemberg MK, Adrain C (2016). "Inactive rhomboid proteins: New mechanisms with implications in health and disease". Semin. Cell Dev. Biol. 60: 29–37. PMID 27378062. doi:10.1016/j.semcdb.2016.06.022. hdl:10400.7/759.
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. PMID 8447824. doi:10.1006/bbrc.1993.1206.
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. PMC 4342846. PMID 25664608. doi:10.1021/acs.biochem.5b00014.

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. PMID 28453015. doi:10.1039/C7CP00277G. Arquivado dende o orixinal o 24 de decembro de 2017. Consultado o 25 de agosto de 2021.

sanger.ac.uk

merops.sanger.ac.uk

Protease TEV MEROPS: clan PA, familia C4
Protease de citomegalovirus MEROPS: clan SH, familia S21
Papaína MEROPS: clan CA, familia C1
Protease do virus da hepatite A MEROPS: clan PA, familia C3
Quimotripsina MEROPS: clan PA, familia S1
Seldolisina protease MEROPS: clan SB, familia 53
Protease vasohibina MEROPS: clan CA
Proteosoma MEROPS: clan PB, familia T1
Ornitina aciltransferases MEROPS: clan PE, familia T5
Penicilina acilase G MEROPS: clan PB, familia S45
Penicilina acilase V,MEROPS: clan PB, familia C59
Amidofosforribosiltransferase MEROPS: clan PB, familia C44
Subtilisina MEROPS: clan SB, familia S8
Prolil oligopeptidase MEROPS: clan SC, familia S9

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. PMID 28453015. doi:10.1039/C7CP00277G. Arquivado dende o orixinal o 24 de decembro de 2017. Consultado o 25 de agosto de 2021.

worldcat.org

Devillanova, Francesco A; Du Mont, Woolf-Walther (2013). Handbook of Chalcogen Chemistry. Vol. 1: new perspectives in sulfur, selenium and tellurium (2nd ed.). Cambridge: RSC. ISBN 9781849736237. OCLC 868953797.