Skip to main content

Specificity of Enzymes

  • Chapter
  • First Online:
  • 2149 Accesses

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.

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   79.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   99.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   139.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

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.

    Google Scholar 

  • 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.

    Google Scholar 

  • Arnold FH and Volkov AA. Directed evolution of biocatalysts. Curr Opin Chem Biol, 1999, 3:54–59.

    Google Scholar 

  • Carey FA and Sundberg RJ. Advanced organic chemistry part A: structure and mechanisms. New York, Plenum Press, 1984.

    Google Scholar 

  • Fitzpatrick P, Ringe D and Klibanov A. Computer assisted modeling of subtilisin enatioselectivity in organic solvent. Biotech.Bioeng, 1992, 40:735–742.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • Hilvert D. Design of protein catalysts. Annu. Rev. Biochem., 2013, 82:447–470.

    Google Scholar 

  • Hopmann KH, Hallberg BM and Himo F. Catalytic mechanism of limonene epoxide hydrolase, a theoretical study.J. Am. Chem. Soc., 2005, 127:14339–14347.

    Google Scholar 

  • Keith JM, Larrow JF andJacobsen EN. Practical considerations in kinetic resolution reactions. Advanced Synthesis & Catalysis, 2001, 343(1):5–26.

    Google Scholar 

  • 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.

    Google Scholar 

  • Kiss G, Çelebi-Ölçüm N, Moretti R, Baker D and Houk KN. Computational enzyme design. Angew Chem, Int Ed, 2013, 52:5700–5725.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • Sobolev V, Sorokine A, Prilusky J, Abola EE and Edelman M. Automated analysis of interatomic contacts in proteins. Bioinformatics, 1999, 15:327–332.

    Google Scholar 

  • 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.

    Google Scholar 

  • Tyagi S and Pleiss J. Biochemical profiling in silico – Predicting substrate specificities of large enzyme families. J. Biotechnology, 2006, 124:108–116.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • Wijma HJ and Janssen DB. Computational design gains momentum in enzyme catalysis engineering. FEBS J, 2013, 280:2948–2960.

    Google Scholar 

  • 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..

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Young Je Yoo .

Rights and permissions

Reprints 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

Publish with us

Policies and ethics