Structural highlights
Function
MUTB_PROFR Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and 3-carboxypropyl-CoA (substrate and product analogues) show that the enzyme-substrate interactions change little during the course of the rearrangement reaction, in contrast to the large conformational change on substrate binding. The substrate complex shows a 5'-deoxyadenine molecule in the active site, bound weakly and not attached to the cobalt atom of coenzyme B12, rotated and shifted from its position in the substrate-free adenosylcobalamin complex. The position of Tyralpha89 close to the substrate explains the stereochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.
Crystal structure of substrate complexes of methylmalonyl-CoA mutase.,Mancia F, Smith GA, Evans PR Biochemistry. 1999 Jun 22;38(25):7999-8005. PMID:10387043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mancia F, Smith GA, Evans PR. Crystal structure of substrate complexes of methylmalonyl-CoA mutase. Biochemistry. 1999 Jun 22;38(25):7999-8005. PMID:10387043 doi:10.1021/bi9903852
