DIVERSITY OF CYCLIC UREIDE COMPOUND, DIHYDROPYRIMIDINE, AND HYDANTOIN HYDROLYZING ENZYMES IN BLASTOBACTER SP A17P-4

被引：12

作者：

OGAWA, J ^{[1
]}

HONDA, M ^{[1
]}

SOONG, CL ^{[1
]}

SHIMIZU, S ^{[1
]}

机构：

[1] KYOTO UNIV, DEPT AGR CHEM, SAKYO KU, KYOTO 606, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 10期

基金：

日本学术振兴会;

关键词：

D O I：

10.1271/bbb.59.1960

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：

Two cyclic ureide compound-hydrolyzing enzymes were found in Blastobacter sp, A17p-4, and partially purified, One hydrolyzed 5-substituted hydantoins D-stereospecifically and had dihydropyrimidinase activity. The other was a novel enzyme which should be called an imidase, The imidase preferably hydrolyzed cyclic imide compounds such as glutarimide and succinimide more than cyclic ureide compounds, and produced monoamidated dicarboxylates.

引用

页码：1960 / 1962

页数：3

共 12 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2]

MAGUIRE JH, 1978, DRUG METAB DISPOS, V6, P601

[3] BETA-UREIDOPROPIONASE WITH N-CARBAMOYL-ALPHA-L-AMINO ACID AMIDOHYDROLASE ACTIVITY FROM AN AEROBIC BACTERIUM, PSEUDOMONAS-PUTIDA IFO 12996 [J].