Crystal structure of l-threonine-O-3-phosphate decarboxylase CobC from Sinorhizobium meliloti involved in vitamin B 12 biosynthesis

Vitamin B is involved in many important biochemical reactions for humans, and its deficiency can lead to serious diseases. The industrial production of vitamin B is achieved through microbial fermentation. In this work, we determine the crystal structures of the l-threonine-O-3-phosphate (Thr-P) dec...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 2024-09, Vol.734, p.150767
Main Authors: Jiang, Meiyu, Guo, Shuoxuan, Chen, Xi, Wei, Qinghao, Wang, Mingzhu
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Vitamin B is involved in many important biochemical reactions for humans, and its deficiency can lead to serious diseases. The industrial production of vitamin B is achieved through microbial fermentation. In this work, we determine the crystal structures of the l-threonine-O-3-phosphate (Thr-P) decarboxylase CobC from Sinorhizobium meliloti (SmCobC), an industrial vitamin B -producing bacterium, in apo form and in complex with a reaction intermediate. Our structures supported the Thr-P decarboxylase activity of SmCobC and revealed that the positively charged substrate-binding pocket between the large and small domains determines its substrate selectivity for Thr-P. Moreover, our results provided evidence for the proposition that the AP-P linker is formed by direct incorporation of AP-P in the biosynthetic pathway of vitamin B in S.meliloti.
ISSN:1090-2104
DOI:10.1016/j.bbrc.2024.150767