Abstract
Enzyme-catalyzed reactions provide several advantages such as specificity, high catalytic rate, transition state stabilization, etc., over inorganic catalysts and they have brought revolutionary changes in the synthesis of compounds at the industrial level. Enzymes are biological catalysts that are specific to the substrates and they increase the rate of reaction several folds by decreasing the activation energy. Enzyme provides an active site where the substrate/s can take a proper position and orientation to react and further stabilize the transition state favoring the reaction to proceed. Technological advancements like genetic engineering by using fungi, bacteria, and yeast, led to the development of novel enzymes possessing varied applications and specificities and they are still under exploration for new applications. Understanding the basic concepts of enzyme-catalyzed reactions can provide novel insights into the development of new strategies for designing artificial enzymes as well as the new methods for increasing the yields of enzyme-catalyzed reactions.
This is a preview of subscription content, log in via an institution to check access.
References
Agarwal PK (2005) Role of protein dynamics in reaction rate enhancement by enzymes. J Am Chem Soc 127:15248–15256
Agarwal PK (2006) Enzymes: an integrated view of structure, dynamics and function. Microb Cell Factories 5:2
Agarwal PK, Schultz C, Kalivretenos A, Ghosh B, Broedel SE (2012) Engineering a hyper-catalytic enzyme by photoactivated conformation modulation. J Phys Chem Lett 3:1142–1146
Baldwin J, Chothia C (1979) Hemoglobin—structural changes related to ligand binding and its allosteric mechanism. J Mol Biol 129:175–200
Bauer JA, Zámocká M, Majtán J, Bauerová-Hlinková V (2022) Glucose oxidase, an enzyme “Ferrari”: its structure, function, production and properties in the light of various industrial and biotechnological applications. Biomol Ther 12(3):472. https://doi.org/10.3390/biom12030472. PMID: 35327664; PMCID: PMC8946809
Bruice TC, Benkovic SJ (2000) Chemical basis for enzyme catalysis. Biochemistry 39:6267–6274
Bruno RD, Njar VC (2007) Targeting cytochrome P450 enzymes: a new approach in anti-cancer drug development. Bioorg Med Chem 15(15):5047–5060
Cook RA, Koshland DE (1970) Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. Biochemistry 9:3337–3342
Egler RA, Ahuja SP, Matloub Y (2016) L-asparaginase in the treatment of patients with acute lymphoblastic leukemia. J Pharmacol Pharmacother 7(2):62–71. https://doi.org/10.4103/0976-500X.184769. PMID: 27440950; PMCID: PMC4936081
Fischer E (1894) Einfluss der Configuration auf die Wirkung den Enzyme. Ber Dtsch Chem Ges 27:2985–2993
Frauenfelder H, McMahon BH, Austin RH, Chu K, Groves JT (2001) The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc Natl Acad Sci U S A 98:2370–2374
Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, Kern D (2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450:913–916
Konieczna I, Zarnowiec P, Kwinkowski M, Kolesinska B, Fraczyk J, Kaminski Z, Kaca W (2012) Bacterial urease and its role in long-lasting human diseases. Curr Protein Pept Sci 13(8):789–806. https://doi.org/10.2174/138920312804871094. PMID: 23305365; PMCID: PMC3816311
Levitzki A, Koshland DE (1969) Negative cooperativity in regulatory enzymes. Proc Natl Acad Sci U S A 62:1121–1128
Lisi GP, Loria JP (2016) Solution NMR spectroscopy for the study of enzyme allostery. Chem Rev 116:6323
Nagel ZD, Klinman JP (2009) A 21(st) century revisionist’s view at a turning point in enzymology. Nat Chem Biol 5:543–550
Nagel ZD, Cun SJ, Klinman JP (2013) Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases. J Biol Chem 288:14087–14097
Nelson DL, Cox MM (2008) Lehninger principles of biochemistry, 5th edn. Wh Freeman, New York
Ramanathan A, Agarwal PK (2011) Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis. PLoS Biol 9:e1001193
Robinson PK (2015) Enzymes: principles and biotechnological applications. Essays Biochem 59:1–41. https://doi.org/10.1042/bse0590001. Erratum in: Essays Biochem 2015; 59:75. PMID: 26504249; PMCID: PMC4692135
Shingleton WD, Hodges DJ, Brick P, Cawston TE (1996) Collagenase: a key enzyme in collagen turnover. Biochem Cell Biol 74(6):759–775. https://doi.org/10.1139/o96-083
Singh PK, Shrivastava N, Ojha BK (2019) Enzymes in the meat industry. In: Enzymes in food biotechnology. Academic Press, pp 111–128
Védrine JC (2017) Heterogeneous catalysis on metal oxides. Catalysts 7(11):341. https://doi.org/10.3390/catal7110341
Warshel A, Sharma PK, Kato M, Xiang Y, Liu HB, Olsson MHM (2006) Electrostatic basis for enzyme catalysis. Chem Rev 106:3210–3235
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2024 The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Rao, K.H., Sahoo, S., Gupta, J. (2024). Basic Concepts and Applications of Enzyme-Catalyzed Reactions for Biotechnology. In: Dhagat, S., Jujjavarapu, S.E., Sampath Kumar, N., Mahapatra, C. (eds) Recent Advances in Bioprocess Engineering and Bioreactor Design. Springer, Singapore. https://doi.org/10.1007/978-981-97-1451-3_4
Download citation
DOI: https://doi.org/10.1007/978-981-97-1451-3_4
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-97-1450-6
Online ISBN: 978-981-97-1451-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)