期刊
CRITICAL REVIEWS IN BIOTECHNOLOGY
卷 39, 期 5, 页码 648-664出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/07388551.2019.1594153
关键词
Pyruvate; glyoxylate; L-alanine; bioreceptor; optically active amino acids; peptidoglycan
资金
- Science and Engineering Research Board, New Delhi
- National Program on Micro Air Vehicles, India
Alanine dehydrogenase (AlaDH) (E.C.1.4.1.1) is a microbial enzyme that catalyzes a reversible conversion of L-alanine to pyruvate. Inter-conversion of alanine and pyruvate by AlaDH is central to metabolism in microorganisms. Its oxidative deamination reaction produces pyruvate which plays a pivotal role in the generation of energy through the tricarboxylic acid cycle for sporulation in the microorganisms. Its reductive amination reaction provides a route for the incorporation of ammonia and produces L-alanine which is required for synthesis of the peptidoglycan layer, proteins, and other amino acids. Also, AlaDH helps in redox balancing as its deamination/amination reaction is linked to the reduction/oxidation of NAD(+)/NADH in microorganisms. AlaDH from a few microorganisms can also reduce glyoxylate into glycine (aminoacetate) in a nonreversible reaction. Both its oxidative and reductive reactions exhibit remarkable applications in the pharmaceutical, environmental, and food industries. The literature addressing the characteristics and applications of AlaDH from a wide range of microorganisms is summarized in the current review.
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