REACTIONS OF PARTIALLY PURIFIED TYROSINE PHENOL LYASE WITH THREONINE AND OTHER AMINO-ACIDS

被引：4

作者：

FALEEV, NG

MARTINKOVA, NS

SADOVNIKOVA, MS

SAPOROVSKAYA, MB

BELIKOV, VM

机构：

[1] Institute of Organo-Element Compounds of the Academy of Sciences of the USSR, Moscow, Vavilova

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1979年 / 1卷 / 04期

关键词：

D O I：

10.1016/0141-0229(79)90047-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Both enantiomers of threonine are transformed to α-ketobutyrate with a partially purified preparation of tyrosine phenol lyase from the cells of Escherichia intermedia A-21. Allothreonine does not undergo the same reaction but is, instead, converted to glycine. The action of tyrosine phenol lyase on a number of other α-amino acids was also studied. The inversion of configuration at C-2 due to the exchange of the α-proton is not a general phenomenon. The mechanism of action of tyrosine phenol lyase on d-amino acids is discussed. © 1979.

引用

页码：269 / 272

页数：4

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