Discovery of a Potentially New Subfamily of ELFV Dehydrogenases Effective for l‐Arginine Deamination by Enzyme Mining. Issue 2 (30th October 2017)

• Record Type: Journal Article
• Authors: Wu, Wenjun; Zhang, Ye; Huang, Jinhai; Wu, Yao; Liu, Dehua; Chen, Zhen
• Is Part Of: Biotechnology journal. Volume 13:Issue 2(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-10-30
• Subjects: amino acid dehydrogenase -- arginine dehydrogenase -- de novo pathway design -- ELFV dehydrogenase -- enzyme mining; Biotechnology -- Periodicals; 660.605
• DOI: 10.1002/biot.201700305
• Languages: English
• ISSNs: 1860-6768

Abstract

Abstract : Discovery of enzymes with new functions is very important for de novo pathway design in synthetic biology. Amino acid dehydrogenases catalyze the oxidative deamination of an amino acid to its keto acid, which are widely used for the production of various valuable chemicals. To discover amino acid dehydrogenases with new functions, the authors reevaluate the sequence variability and substrate diversity of ELFV dehydrogenases superfamily in this study. With insights gained from structural and sequential studies, the authors develop an in silico strategy and discover a new category of proteins which are originally annotated as glutamate dehydrogenase but show altered conservation pattern of specificity determined motifs and completely different substrate spectrum. These proteins cannot catalyze the deamination of glutamate and other canonical amino acids except the positively charged amino acidl ‐arginine, representing a potentially new subfamily of ELFV dehydrogenases. The strategy utilized in this study can also be applied for discovering other useful enzymes. Abstract : Discovery of enzymes with new functions is very important for de novo pathway design in synthetic biology. In this study, the authors demonstrate that combining structural and sequential alignment and specificity determined motifs for enzyme reannotation and to discover new amino acid dehydrogenases which can effectively catalyze the deamination of arginine. This strategy developed in this work can be used to discover other new enzymes/enzyme functions and reclassification of enzymes.