STEREOCHEMISTRY OF REACTIONS CATALYZED BY MAMMALIAN-BRAIN L-GLUTAMATE 1-CARBOXY-LYASE AND 4-AMINOBUTYRATE - 2-OXOGLUTARATE AMINOTRANSFERASE

被引：42
作者：
BOUCLIER, M
JUNG, MJ
LIPPERT, B
机构：
[1] Centre de Recherche Merrell International, Strasbourg, F-67084
[2] Merrell Research Center, Merrell National Laboratories, Cincinnati, Ohio, 45215
来源：
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 98卷 / 02期
关键词：
D O I：
10.1111/j.1432-1033.1979.tb13195.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Deamination of 4‐aminobutyrate by mammalian or bacterial 4‐aminobutyrate aminotransferases involves the abstraction of the pro‐S hydrogen on C‐4 of 4‐aminobutyrate. Decarboxylation of L‐glutamate by rat brain glutamate decarboxylase occurs with retention of configuration. Inhibition of this enzyme by (S)‐4‐aminohex‐5‐ynoic acid involves the abstraction of the proton at C‐4 of the inhibitor. On the basis of this finding, we postulate the existence of an abnormal reaction of glutamate decarboxylase in which the proton at C‐4 of (S)‐4‐aminohex‐5‐ynoic acid is removed in a manner similar to the one which normally occurs in enzymatic transaminations of L‐amino acids. This reaction is presumably facilitated by the acetylenic group adjacent to the eliminated proton. Copyright © 1979, Wiley Blackwell. All rights reserved
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页码：363 / 368
页数：6
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