STEREOCHEMISTRY OF HYDROGEN ELIMINATION IN ENZYMIC FORMATION OF C-2-C-3 DOUBLE-BOND OF PORPHOBILINOGEN

被引：11

作者：

ABBOUD, MM ^{[1
]}

AKHTAR, M ^{[1
]}

机构：

[1] UNIV SOUTHAMPTON, DEPT PHYSIOL & BIOCHEM, SOUTHAMPTON SO9 3TU, ENGLAND

来源：

JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS | 1976年 / 24期

关键词：

D O I：

10.1039/c39760001007

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Using 5-aminolevulinate dehydratase from Rhodopseudomonas spheroides it is shown that the tritium located in the pro-S position at C-5 of 5-aminolevulinate is retained at C-2 of porphobilinogen.

引用

页码：1007 / 1008

页数：2

共 4 条

[1] BIOSYNTHESIS OF 5-AMINOLEVULINIC ACID - INVOLVEMENT OF A RETENTION-INVERSION MECHANISM
ABBOUD, MM
JORDAN, PM
AKHTAR, M
[J]. JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS, 1974, (16) : 643 - 644
[2] MECHANISM AND STEREOCHEMISTRY OF ENZYMIC REACTIONS INVOLVED IN PORPHYRIN BIOSYNTHESIS
AKHTAR, M
ABBOUD, MM
BARNARD, G
JORDAN, P
ZAMAN, Z
[J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1976, 273 (924) : 117 - 136
[3] CHAUDHRY AG, IN PRESS
[4] NANDI DL, 1968, J BIOL CHEM, V243, P1236

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