Crystal structure of substrate complexes of methylmalonyl-CoA mutase
Crystal structure of substrate complexes of methylmalonyl-CoA mutase
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DOI：
10.1021/bi9903852
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发表时间：
1999-06-22
期刊：
影响因子：
2.9
通讯作者：
Evans, PR
中科院分区：
文献类型：
--
作者：
Mancia, F;Smith, GA;Evans, PR
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 B-12, rotated and shifted from its position in the substrate-free adenosylcobalamin complex. The position of Tyr alpha 89 close to the substrate explains the stereochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA.
