Journal
CRITICAL REVIEWS IN BIOTECHNOLOGY
Volume 39, Issue 3, Pages 366-379Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/07388551.2019.1566205
Keywords
Alcohol dehydrogenase; structure; function; characteristics; molecular mechanism; asymmetric biotransformation
Categories
Funding
- National Natural Science Foundation of China (NSFC) [21336009, 21676120, 31872891]
- Natural Science Foundation of Jiangsu Province [BK20151124]
- 111 Project [111-2-06]
- High-end Foreign Experts Recruitment Program [GDT20183200136]
- Program for Advanced Talents within Six Industries of Jiangsu Province [2015-NY-007]
- National Program for Support of Top-notch Young Professionals
- Fundamental Research Funds for the Central Universities [JUSRP51504]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- Jiangsu province Collaborative Innovation Center for Advanced Industrial Fermentation industry development program
- Top-notch Academic Programs Project of Jiangsu Higher Education Institutions
- National First-Class Discipline Program of Light Industry Technology and Engineering [LITE2018-09]
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Alcohol dehydrogenases are a group of oxidoreductases that specifically use NAD(P)(+) or NAD(P)H as cofactors for electron acceptance or donation and catalyze interconversion between alcohols and corresponding carbonyl compounds. In addition to their physiological roles in metabolizing alcohols and aldehydes or ketones, alcohol dehydrogenases have received considerable attention with respect to their symmetry-breaking traits in catalyzing asymmetric reactions and have Accordingly, they have become widely applied in fine chemical synthesis, particularly in the production of chiral alcohols and hydroxyl compounds that are key elements in the synthesis of active pharmaceutical ingredients (API) employed in the pharmaceutical industry. The application of structural bioinformatics to the study of functional enzymes and recent scientific breakthroughs in modern molecular biotechnology provide us with an effective alternative to gain an understanding of the molecular mechanisms involved in asymmetric bioreactions and in overcoming the limitations of enzyme availability. In this review, we discuss molecular mechanisms underlying alcohol dehydrogenase-mediated asymmetric reactions, based on protein structure-function relationships from domain structure to functional active sites. The molecular principles of the catalytic machinery involving stereochemical recognition and molecular interaction are also addressed. In addition, the diversity of enzymatic functions and properties, for example, enantioselectivity, substrate specificity, cofactor dependence, metal requirement, and stability in terms of organic solvent tolerance and thermostability, are also discussed and based on a comparative analysis of high-resolution 3D structures of representative alcohol dehydrogenases.
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