9JFB

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

(2024) Biochem Biophys Res Commun 734: 150767-150767

• PubMed: 39366178 Search on PubMed
• DOI: https://doi.org/10.1016/j.bbrc.2024.150767
• Primary Citation of Related Structures:  
  9JFB, 9JFF


• PubMed Abstract: 
  

  Vitamin B ₁₂ is involved in many important biochemical reactions for humans, and its deficiency can lead to serious diseases. The industrial production of vitamin B ₁₂ 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 ₁₂ -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 ₁₂ in S.meliloti.

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Organizational Affiliation: 

Institutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, Anhui, China; School of Life Sciences, Anhui University, Hefei, 230601, Anhui, China.