Fischer E (1894). "Einfluss der Configuration auf die Wirkung der Enzyme" [Influence of configuration on the action of enzymes]. Berichte der Deutschen Chemischen Gesellschaft zu Berlin (in German). 27 (3): 2985–93. doi:10.1002/cber.18940270364. From page 2992: "Um ein Bild zu gebrauchen, will ich sagen, dass Enzym und Glucosid wie Schloss und Schlüssel zu einander passen müssen, um eine chemische Wirkung auf einander ausüben zu können." (To use an image, I will say that an enzyme and a glucoside [i.e., glucose derivative] must fit like a lock and key, in order to be able to exert a chemical effect on each other.)
Kühne coined the word "enzyme" in: Kühne W (1877). "Über das Verhalten verschiedener organisirter und sog. ungeformter Fermente" [On the behavior of various organized and so-called unformed ferments]. Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg. new series (in German). 1 (3): 190–193. Relevant passage on page 190: "Um Missverständnissen vorzubeugen und lästige Umschreibungen zu vermeiden schlägt Vortragender vor, die ungeformten oder nicht organisirten Fermente, deren Wirkung ohne Anwesenheit von Organismen und ausserhalb derselben erfolgen kann, als Enzyme zu bezeichnen." (Translation: In order to obviate misunderstandings and avoid cumbersome periphrases, [the author, a university lecturer] suggests designating as "enzymes" the unformed or not organized ferments, whose action can occur without the presence of organisms and outside of the same.)
Holmes FL (2003). "Enzymes". In Heilbron JL (ed.). The Oxford Companion to the History of Modern Science. Oxford: Oxford University Press. p. 270. ISBN9780199743766.
The naming of enzymes by adding the suffix "-ase" to the substrate on which the enzyme acts, has been traced to French scientist Émile Duclaux (1840–1904), who intended to honor the discoverers of diastase – the first enzyme to be isolated – by introducing this practice in his book Duclaux E (1899). Traité de microbiologie: Diastases, toxines et venins [Microbiology Treatise: diastases, toxins and venoms] (in French). Paris, France: Masson and Co. See Chapter 1, especially page 9.
Murphy JM, Farhan H, Eyers PA (April 2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochemical Society Transactions. 45 (2): 537–544. doi:10.1042/bst20160400. PMID28408493.
Manchester KL (December 1995). "Louis Pasteur (1822–1895)--chance and the prepared mind". Trends in Biotechnology. 13 (12): 511–515. doi:10.1016/S0167-7799(00)89014-9. PMID8595136.
Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR (May 1965). "Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution". Nature. 206 (4986): 757–761. Bibcode:1965Natur.206..757B. doi:10.1038/206757a0. PMID5891407. S2CID4161467.
Johnson LN, Petsko GA (July 1999). "David Phillips and the origin of structural enzymology". Trends in Biochemical Sciences. 24 (7): 287–289. doi:10.1016/S0968-0004(99)01423-1. PMID10390620.
Rodnina MV, Wintermeyer W (2001). "Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms". Annual Review of Biochemistry. 70: 415–435. doi:10.1146/annurev.biochem.70.1.415. PMID11395413.
Fischer E (1894). "Einfluss der Configuration auf die Wirkung der Enzyme" [Influence of configuration on the action of enzymes]. Berichte der Deutschen Chemischen Gesellschaft zu Berlin (in German). 27 (3): 2985–93. doi:10.1002/cber.18940270364. From page 2992: "Um ein Bild zu gebrauchen, will ich sagen, dass Enzym und Glucosid wie Schloss und Schlüssel zu einander passen müssen, um eine chemische Wirkung auf einander ausüben zu können." (To use an image, I will say that an enzyme and a glucoside [i.e., glucose derivative] must fit like a lock and key, in order to be able to exert a chemical effect on each other.)
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis". Chemical Reviews. 106 (8): 3210–3235. doi:10.1021/cr0503106. PMID16895325.
Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates". Accounts of Chemical Research. 47 (1): 149–156. doi:10.1021/ar400084s. OSTI1565147. PMID23988159.
Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity". Trends in Biochemical Sciences. 24 (9): 359–363. doi:10.1016/s0968-0004(99)01438-3. PMID10470036.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, et al. (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II". Biochemistry. 44 (4): 1097–1105. doi:10.1021/bi0480279. PMID15667203.
Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R (May 2011). "The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters". Biochemistry. 50 (21): 4402–4410. doi:10.1021/bi2002289. PMID21506553.
Ellis RJ (October 2001). "Macromolecular crowding: obvious but underappreciated". Trends in Biochemical Sciences. 26 (10): 597–604. doi:10.1016/S0968-0004(01)01938-7. PMID11590012.
Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design". Annual Review of Biophysics and Biomolecular Structure. 27: 249–284. doi:10.1146/annurev.biophys.27.1.249. PMID9646869. S2CID10205781.
De Clercq E (April 2002). "Highlights in the development of new antiviral agents". Mini Reviews in Medicinal Chemistry. 2 (2): 163–175. doi:10.2174/1389557024605474. PMID12370077.
Murzin AG (November 1993). "Can homologous proteins evolve different enzymatic activities?". Trends in Biochemical Sciences. 18 (11): 403–405. doi:10.1016/0968-0004(93)90132-7. PMID8291080.
Ochoa D, Bradley D, Beltrao P (February 2018). "Evolution, dynamics and dysregulation of kinase signalling". Current Opinion in Structural Biology. 48: 133–140. doi:10.1016/j.sbi.2017.12.008. PMID29316484.
Renugopalakrishnan V, Garduño-Juárez R, Narasimhan G, Verma CS, Wei X, Li P (November 2005). "Rational design of thermally stable proteins: relevance to bionanotechnology". Journal of Nanoscience and Nanotechnology. 5 (11): 1759–1767. doi:10.1166/jnn.2005.441. PMID16433409.
Hult K, Berglund P (August 2003). "Engineered enzymes for improved organic synthesis". Current Opinion in Biotechnology. 14 (4): 395–400. doi:10.1016/S0958-1669(03)00095-8. PMID12943848.
Kirk O, Borchert TV, Fuglsang CC (August 2002). "Industrial enzyme applications". Current Opinion in Biotechnology. 13 (4): 345–351. doi:10.1016/S0958-1669(02)00328-2. PMID12323357.
Guzmán-Maldonado H, Paredes-López O (September 1995). "Amylolytic enzymes and products derived from starch: a review". Critical Reviews in Food Science and Nutrition. 35 (5): 373–403. doi:10.1080/10408399509527706. PMID8573280.
Alkorta I, Garbisu C, Llama MJ, Serra JL (January 1998). "Industrial applications of pectic enzymes: a review". Process Biochemistry. 33 (1): 21–28. doi:10.1016/S0032-9592(97)00046-0.
Murphy JM, Farhan H, Eyers PA (April 2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochemical Society Transactions. 45 (2): 537–544. doi:10.1042/bst20160400. PMID28408493.
Manchester KL (December 1995). "Louis Pasteur (1822–1895)--chance and the prepared mind". Trends in Biotechnology. 13 (12): 511–515. doi:10.1016/S0167-7799(00)89014-9. PMID8595136.
Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR (May 1965). "Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution". Nature. 206 (4986): 757–761. Bibcode:1965Natur.206..757B. doi:10.1038/206757a0. PMID5891407. S2CID4161467.
Johnson LN, Petsko GA (July 1999). "David Phillips and the origin of structural enzymology". Trends in Biochemical Sciences. 24 (7): 287–289. doi:10.1016/S0968-0004(99)01423-1. PMID10390620.
Rodnina MV, Wintermeyer W (2001). "Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms". Annual Review of Biochemistry. 70: 415–435. doi:10.1146/annurev.biochem.70.1.415. PMID11395413.
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis". Chemical Reviews. 106 (8): 3210–3235. doi:10.1021/cr0503106. PMID16895325.
Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates". Accounts of Chemical Research. 47 (1): 149–156. doi:10.1021/ar400084s. OSTI1565147. PMID23988159.
Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity". Trends in Biochemical Sciences. 24 (9): 359–363. doi:10.1016/s0968-0004(99)01438-3. PMID10470036.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, et al. (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II". Biochemistry. 44 (4): 1097–1105. doi:10.1021/bi0480279. PMID15667203.
Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R (May 2011). "The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters". Biochemistry. 50 (21): 4402–4410. doi:10.1021/bi2002289. PMID21506553.
Ellis RJ (October 2001). "Macromolecular crowding: obvious but underappreciated". Trends in Biochemical Sciences. 26 (10): 597–604. doi:10.1016/S0968-0004(01)01938-7. PMID11590012.
Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design". Annual Review of Biophysics and Biomolecular Structure. 27: 249–284. doi:10.1146/annurev.biophys.27.1.249. PMID9646869. S2CID10205781.
De Clercq E (April 2002). "Highlights in the development of new antiviral agents". Mini Reviews in Medicinal Chemistry. 2 (2): 163–175. doi:10.2174/1389557024605474. PMID12370077.
Murzin AG (November 1993). "Can homologous proteins evolve different enzymatic activities?". Trends in Biochemical Sciences. 18 (11): 403–405. doi:10.1016/0968-0004(93)90132-7. PMID8291080.
Ochoa D, Bradley D, Beltrao P (February 2018). "Evolution, dynamics and dysregulation of kinase signalling". Current Opinion in Structural Biology. 48: 133–140. doi:10.1016/j.sbi.2017.12.008. PMID29316484.
Renugopalakrishnan V, Garduño-Juárez R, Narasimhan G, Verma CS, Wei X, Li P (November 2005). "Rational design of thermally stable proteins: relevance to bionanotechnology". Journal of Nanoscience and Nanotechnology. 5 (11): 1759–1767. doi:10.1166/jnn.2005.441. PMID16433409.
Hult K, Berglund P (August 2003). "Engineered enzymes for improved organic synthesis". Current Opinion in Biotechnology. 14 (4): 395–400. doi:10.1016/S0958-1669(03)00095-8. PMID12943848.
Kirk O, Borchert TV, Fuglsang CC (August 2002). "Industrial enzyme applications". Current Opinion in Biotechnology. 13 (4): 345–351. doi:10.1016/S0958-1669(02)00328-2. PMID12323357.
Guzmán-Maldonado H, Paredes-López O (September 1995). "Amylolytic enzymes and products derived from starch: a review". Critical Reviews in Food Science and Nutrition. 35 (5): 373–403. doi:10.1080/10408399509527706. PMID8573280.
Begley CG, Paragina S, Sporn A (March 1990). "An analysis of contact lens enzyme cleaners". Journal of the American Optometric Association. 61 (3): 190–194. PMID2186082.
Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates". Accounts of Chemical Research. 47 (1): 149–156. doi:10.1021/ar400084s. OSTI1565147. PMID23988159.
qmul.ac.uk
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Nomenclature Committee. "EC 2.7.1.1". International Union of Biochemistry and Molecular Biology (NC-IUBMB). School of Biological and Chemical Sciences, Queen Mary, University of London. Archived from the original on 1 December 2014. Retrieved 6 March 2015.
Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design". Annual Review of Biophysics and Biomolecular Structure. 27: 249–284. doi:10.1146/annurev.biophys.27.1.249. PMID9646869. S2CID10205781.
Nomenclature Committee. "EC 2.7.1.1". International Union of Biochemistry and Molecular Biology (NC-IUBMB). School of Biological and Chemical Sciences, Queen Mary, University of London. Archived from the original on 1 December 2014. Retrieved 6 March 2015.
Boyer R (2002). "Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition". Concepts in Biochemistry (2nd ed.). New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. pp. 137–8. ISBN0-470-00379-0. OCLC51720783.
Bisswanger H (2017). Enzyme kinetics : principles and methods (Third, enlarged and improved ed.). Weinheim, Germany: Wiley-VCH. ISBN9783527806461. OCLC992976641.
Jain JL (May 1999). Fundamentals of biochemistry. New Delhi: S. Chand and Co. ISBN8121903432. OCLC818809626.