EVIDENCE FOR A MECHANISM INVOLVING TRANSIENT FRAGMENTATION IN CARBON SKELETON REARRANGEMENTS DEPENDENT ON COENZYME B-12

被引:65
作者
BEATRIX, B
ZELDER, O
KROLL, FK
ORLYGSSON, G
GOLDING, BT
BUCKEL, W
机构
[1] UNIV MARBURG, FACHBEREICH BIOL, MIKROBIOL LAB, D-35032 MARBURG, GERMANY
[2] UNIV NEWCASTLE UPON TYNE, DEPT CHEM, NEWCASTLE UPON TYNE NE1 7RU, TYNE & WEAR, ENGLAND
关键词
COENZYME B-12; ENZYME CATALYSIS; REARRANGEMENTS;
D O I
10.1002/anie.199523981
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Enzyme kinetics and EPR spectroscopy provide evidence that in the reversible rearrangement of (S)‐glutamate (1) to (2S, 3S)‐3‐methylaspartate (2), which is catalyzed by the coenzyme B12 dependent glutamate mutase from Clostridium cochlearium, the substrate 1 fragments into acrylate (3) and glycine radical (4), which recombine to 2. Ado‐CH2‐Cbl  5′‐adenosylcobalamin (coenzyme B12). (Figure Presented.) Copyright © 1995 by VCH Verlagsgesellschaft mbH, Germany
引用
收藏
页码:2398 / 2401
页数:4
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