This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6req
From Proteopedia
|
METHYLMALONYL-COA MUTASE, 3-CARBOXYPROPYL-COA INHIBITOR COMPLEX
Overview
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.
About this Structure
6REQ is a Protein complex structure of sequences from Propionibacterium freudenreichii subsp. shermanii with 3CP, B12 and GOL as ligands. Active as Methylmalonyl-CoA mutase, with EC number 5.4.99.2 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 15:25:39 2007
