|
type |
Journal Article |
authors |
Zhu Y, Xu J, Mei X, Feng Z, Zhang L, Zhang Q, Zhang G, Zhu W, Liu J, Zhang C. |
title |
Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis. |
journal |
ACS Chem Biol. |
Activity |
crmg |
Family |
crmg |
sel |
selected |
ui |
26714051 |
year |
(2016) |
volume |
11 |
number |
4 |
pages |
943-52 |
| |
abstract |
Caerulomycin A (CRM A 1) belongs to a family of natural products containing a 2,2'-bipyridyl ring core structure and is currently under development as a potent novel immunosuppressive agent. Herein, we report the functional characterization, kinetic analysis, substrate specificity, and structure insights of an aminotransferase CrmG in 1 biosynthesis. The aminotransferase CrmG was confirmed to catalyze a key transamination reaction to convert an aldehyde group to an amino group in the 1 biosynthetic pathway, preferring l-glutamate and l-glutamine as the amino donor substrates. The crystal structures of CrmG in complex with the cofactor 5'-pyridoxal phosphate (PLP) or 5'-pyridoxamine phosphate (PMP) or the acceptor substrate were determined to adopt a canonical fold-type I of PLP-dependent enzymes with a unique small additional domain. The structure guided site-directed mutagenesis identified key amino acid residues for substrate binding and catalytic activities, thus providing insights into the transamination mechanism of CrmG. |
last changed |
2019/03/25 14:15 |
|