Boyer R. Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition. Concepts in Biochemistry 2nd. New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. 2002: 137–8. ISBN 0-470-00379-0. OCLC 51720783.
Fischer E. Einfluss der Configuration auf die Wirkung der Enzyme [Influence of configuration on the action of enzymes]. Berichte der Deutschen chemischen Gesellschaft zu Berlin. 1894, 27 (3): 2985–93 [2007-09-27]. doi:10.1002/cber.18940270364. (原始内容存档于2011-05-11) (德语). 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.)
Jaeger KE, Eggert T. Enantioselective biocatalysis optimized by directed evolution. Current Opinion in Biotechnology. August 2004, 15 (4): 305–13. PMID 15358000. doi:10.1016/j.copbio.2004.06.007.
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O'Brien PJ, Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chemistry & Biology. April 1999, 6 (4): R91–R105. PMID 10099128. doi:10.1016/S1074-5521(99)80033-7.
Fischer E. Einfluss der Configuration auf die Wirkung der Enzyme [Influence of configuration on the action of enzymes]. Berichte der Deutschen chemischen Gesellschaft zu Berlin. 1894, 27 (3): 2985–93 [2007-09-27]. doi:10.1002/cber.18940270364. (原始内容存档于2011-05-11) (德语). 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. Electrostatic basis for enzyme catalysis. Chemical Reviews. August 2006, 106 (8): 3210–35. PMID 16895325. doi:10.1021/cr0503106.
Chapman-Smith A, Cronan JE. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends Biochem. Sci. 1999, 24 (9): 359–63. PMID 10470036. doi:10.1016/s0968-0004(99)01438-3.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry. February 2005, 44 (4): 1097–115. PMID 15667203. doi:10.1021/bi0480279.
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doi.org
Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus, ChemBioChem, 2017, 18(19):1944-1949https://doi.org/10.1002/cbic.201700258
Jaeger KE, Eggert T. Enantioselective biocatalysis optimized by directed evolution. Current Opinion in Biotechnology. August 2004, 15 (4): 305–13. PMID 15358000. doi:10.1016/j.copbio.2004.06.007.
Shevelev IV, Hübscher U. The 3' 5' exonucleases. Nature Reviews Molecular Cell Biology. May 2002, 3 (5): 364–76. PMID 11988770. doi:10.1038/nrm804.
O'Brien PJ, Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chemistry & Biology. April 1999, 6 (4): R91–R105. PMID 10099128. doi:10.1016/S1074-5521(99)80033-7.
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH. Electrostatic basis for enzyme catalysis. Chemical Reviews. August 2006, 106 (8): 3210–35. PMID 16895325. doi:10.1021/cr0503106.
Chapman-Smith A, Cronan JE. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends Biochem. Sci. 1999, 24 (9): 359–63. PMID 10470036. doi:10.1016/s0968-0004(99)01438-3.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry. February 2005, 44 (4): 1097–115. PMID 15667203. doi:10.1021/bi0480279.
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Renugopalakrishnan V, Garduño-Juárez R, Narasimhan G, Verma CS, Wei X, Li P. Rational design of thermally stable proteins: relevance to bionanotechnology. Journal of Nanoscience and Nanotechnology. November 2005, 5 (11): 1759–1767. PMID 16433409. doi:10.1166/jnn.2005.441.
Hult K, Berglund P. Engineered enzymes for improved organic synthesis. Current Opinion in Biotechnology. August 2003, 14 (4): 395–400. PMID 12943848. doi:10.1016/S0958-1669(03)00095-8.
Sun Y, Cheng J. Hydrolysis of lignocellulosic materials for ethanol production: a review. Bioresource Technology. May 2002, 83 (1): 1–11. PMID 12058826. doi:10.1016/S0960-8524(01)00212-7.
Guzmán-Maldonado H, Paredes-López O. Amylolytic enzymes and products derived from starch: a review. Critical Reviews in Food Science and Nutrition. September 1995, 35 (5): 373–403. PMID 8573280. doi:10.1080/10408399509527706.
Bajpai P. Application of enzymes in the pulp and paper industry. Biotechnology Progress. March 1999, 15 (2): 147–157. PMID 10194388. doi:10.1021/bp990013k.
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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. [2016-08-16]. (原始内容存档于2014-12-01).
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. [2016-08-16]. (原始内容存档于2014-12-01).
Fischer E. Einfluss der Configuration auf die Wirkung der Enzyme [Influence of configuration on the action of enzymes]. Berichte der Deutschen chemischen Gesellschaft zu Berlin. 1894, 27 (3): 2985–93 [2007-09-27]. doi:10.1002/cber.18940270364. (原始内容存档于2011-05-11) (德语). 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.)
Boyer R. Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition. Concepts in Biochemistry 2nd. New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. 2002: 137–8. ISBN 0-470-00379-0. OCLC 51720783.