Structural highlights
FunctionPublication Abstract from PubMedAmine compounds biosynthesis using omega-transaminases has received considerable attention in the pharmaceutical industry. However, the application of omega-transaminases was hampered by the fundamental challenge of severe by-product inhibition. Here, we report that omega-transaminase CrmG from Actinoalloteichus cyanogriseus WH1-2216-6 is insensitive to inhibition from by-product alpha-ketoglutarate or pyruvate. Combined with structural and QM/MM studies, we establish the detailed catalytic mechanism for CrmG. Our structural and biochemical studies reveal that the roof of the active site in PMP-bound CrmG is flexible, which will facilitate the PMP or by-product to dissociate from PMP-bound CrmG. Our results also show that amino acceptor caerulomycin M (CRM M), but not alpha-ketoglutarate or pyruvate, can form strong interactions with the roof of the active site in PMP-bound CrmG. Based on our results, we propose that the flexible roof of the active site in PMP-bound CrmG may facilitate CrmG to overcome inhibition from the by-product. Structural studies reveal flexible roof of active site responsible for omega-transaminase CrmG overcoming by-product inhibition.,Xu J, Tang X, Zhu Y, Yu Z, Su K, Zhang Y, Dong Y, Zhu W, Zhang C, Wu R, Liu J Commun Biol. 2020 Aug 19;3(1):455. doi: 10.1038/s42003-020-01184-w. PMID:32814814[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 10:06, 22 November 2023.