Structural highlights
Publication Abstract from PubMed
Structure-based engineering of a NAD+-dependent secondary alcohol dehydrogenase from Micrococcus luteus led to a 1800-fold increase in catalytic efficiency for NADP+. Furthermore, the engineered enzymes (e.g., D37S/A38R/V39S/T15I) were successfully coupled to a NADPH-dependent Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440 for redox-neutral biotransformations of C18 fatty acids into C9 chemicals.
Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids.,Seo EJ, Kim HJ, Kim MJ, Kim JS, Park JB Chem Commun (Camb). 2019 Nov 28;55(96):14462-14465. doi: 10.1039/c9cc06447h. PMID:31728457[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seo EJ, Kim HJ, Kim MJ, Kim JS, Park JB. Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids. Chem Commun (Camb). 2019 Nov 28;55(96):14462-14465. doi: 10.1039/c9cc06447h. PMID:31728457 doi:http://dx.doi.org/10.1039/c9cc06447h
