Abstract
The enzymatic reaction starts with the binding of the substrate to the enzyme. When the substrate approaches to the active site of enzyme, the electrostatic microenvironment in the substrate-binding region changes to make the reaction proceeds to form the final products.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Andrews FH and McLeish MJ. Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes. FEBS J, 2013, 280:6395–6411.
Antipov E, Cho AE and Klibanov AM. How a single-point mutation in horseradish peroxidase markedly enhances enantioselectivity. J. Am. Chem. Soc., 2009, 131:11155–11160.
Arnold FH and Volkov AA. Directed evolution of biocatalysts. Curr Opin Chem Biol, 1999, 3:54–59.
Carey FA and Sundberg RJ. Advanced organic chemistry part A: structure and mechanisms. New York, Plenum Press, 1984.
Fitzpatrick P, Ringe D and Klibanov A. Computer assisted modeling of subtilisin enatioselectivity in organic solvent. Biotech.Bioeng, 1992, 40:735–742.
Gao X, Huang F, Feng J, Chen X, Zhang H, Wang Z, Wu Q and Zhu D. Engineering the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum by site saturation mutagenesis for d-phenylalanine synthesis. Appl Environ Microbiol, 2013, 79:5078–5081.
Gordon SR, Stanley EJ, Wolf S, Toland A, Wu SJ, Hadidi D, Mills JH, Baker D, Pultz IS and Siegel JB. Computational design of an α-gliadin peptidase. J Am Chem Soc, 2012, 134:20513–20520.
Hilvert D. Design of protein catalysts. Annu. Rev. Biochem., 2013, 82:447–470.
Hopmann KH, Hallberg BM and Himo F. Catalytic mechanism of limonene epoxide hydrolase, a theoretical study.J. Am. Chem. Soc., 2005, 127:14339–14347.
Keith JM, Larrow JF andJacobsen EN. Practical considerations in kinetic resolution reactions. Advanced Synthesis & Catalysis, 2001, 343(1):5–26.
Khare SD, Kipnis Y, Greisen PJ, Takeuchi R, Ashani Y, Goldsmith M, Song Y, Gallaher JL, Silman I, Leader H. Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis. Nat Chem Biol, 2012, 8:294–300.
Kiss G, Çelebi-Ölçüm N, Moretti R, Baker D and Houk KN. Computational enzyme design. Angew Chem, Int Ed, 2013, 52:5700–5725.
Manna SK and Mazumdar S. Tuning the substrate specificity by engineering the active site of cytochrome P450cam: A rational approach. Dalton Trans, 2010, 39:3115–3123.
Mouratou B, Kasper P, Gehring H and Christen, P. Conversion of tyrosine phenol-lyase to dicarboxylic amino acid β- lyase, an enzyme not found in nature. J Biol Chem, 1999, 274:1320–1325.
Murphy PM, Bolduc JM, Gallaher JL, Stoddard BL and Baker D. Alteration of enzyme specificity by computational loop remodeling and design. Proc Natl Acad Sci U S A, 2009, 106:9215–9220.
Otten LG, Hollmann F and Arends IW. Enzyme engineering for enantioselectivity: from trial-and-error to rational design? Trends in Biotechnology, 2009, 28(1):46–54.
Rouhi M. Chiral Chemistry: Traditional methods thrive despite numerous hurdles, including tough luck, slow commercialization of catalytic processes. Chemical & Engineering News, 2004, 82:47–62.
Schmid A, Hollmann F, Park JB and Bühler B. The use of enzymes in the chemical industry in Europe. Current Opinion in Biotechnology, 2002, 13:359–366.
Sinclair R, Reid GA and Chapman SK. Re-design of Saccharomyces cerevisiae flavocytochrome b2: Introduction of L-mandelate dehydrogenase activity. Biochem J, 1998, 333:117–120.
Sobolev V, Sorokine A, Prilusky J, Abola EE and Edelman M. Automated analysis of interatomic contacts in proteins. Bioinformatics, 1999, 15:327–332.
Strauss UT, Felfer U and Faber K. Biocatalytic transformation of racemates into chiral building blocks in 100% chemical yield and 100% enantiomeric excess. Tetrahedron-Asymmetry, 1999, 10(1):107–117.
Tyagi S and Pleiss J. Biochemical profiling in silico – Predicting substrate specificities of large enzyme families. J. Biotechnology, 2006, 124:108–116.
Tyka MD, Jung K and Baker D. Efficient sampling of protein conformational space using fast loop building and batch minimization on highly parallel computers. J Comput Chem, 2012, 33:2483–2491.
Watanabe S, Kodaki T and Makino K. Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc. J. Biol. Chem, 2005, 280:10340–10349.
Wijma HJ and Janssen DB. Computational design gains momentum in enzyme catalysis engineering. FEBS J, 2013, 280:2948–2960.
Wijma HJ, Floor RJ, Bjelic S, Marrink SJ and Baker D. Enantioselective enzymes by computational design and in silico screening. Angewandte Chemie, 2015, 127:3797–3801..
Xie T, Song B, Yue Y, Chao Y and Qian S. Site-saturation mutagenesis of central tyrosine 195 leading to diverse product specificities of an α-cyclodextrin glycosyltransferase from Paenibacillus sp. 602–1. J Biotechnol, 2014, 170:10-16.
Yeon YJ, Park HY and Yoo YJ. Enzymatic reduction of levulinic acid by engineering the substrate specificity of 3-hydroxybutyrate dehydrogenase. Bioresource Technology, 2013, 134:377–380.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2017 Springer Science+Business Media B.V.
About this chapter
Cite this chapter
Yoo, Y.J., Feng, Y., Kim, Y.H., Yagonia, C.F.J. (2017). Specificity of Enzymes. In: Fundamentals of Enzyme Engineering. Springer, Dordrecht. https://doi.org/10.1007/978-94-024-1026-6_10
Download citation
DOI: https://doi.org/10.1007/978-94-024-1026-6_10
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-024-1024-2
Online ISBN: 978-94-024-1026-6
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)