Aminoaldehyde dehydrogenase of pea epicotyls

被引：14

作者：

Awal, HMA

Kinoshita, T

Yoshida, I

Doe, M

Hirasawa, E

机构：

[1] OSAKA CITY UNIV,FAC SCI,DEPT BIOL,SUMIYOSHI KU,OSAKA 558,JAPAN

[2] OSAKA CITY UNIV,FAC SCI,DEPT CHEM,SUMIYOSHI KU,OSAKA 558,JAPAN

来源：

PHYTOCHEMISTRY | 1997年 / 44卷 / 06期

关键词：

Pisum sativum; leguminosae; pea epicotyl; aminoaldehyde dehydrogenase; 1,5-diazabicyclo[4.3.0]nonane;

D O I：

10.1016/S0031-9422(96)00678-4

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：

NAD-dependent aminoaldehyde dehydrogenase was partially purified ca 110-fold from pea epicotyls. The purified enzyme (M(r) ca 82 000) catalysed the oxidation of 1,5-diazabicyclo[4.3.0]nonane (1,5-DBN) to N-(3-aminopropyl)-2-pyrrolidinone. The K-m values were 1.0 x 10(-4) M for 1,5-DBN, 2.6 x 10(-5) M for 3-aminopropionaldehyde (3-APA), 1.2 x 10(-4) M for 4-aminobutyraldehyde, 2.2 x 10(-4) M for indole-3-acetaldehyde and 3.7 x 10(-5) M for NAD (in the case of 3-APA). The enzyme had some activity for an aldehyde from spermine oxidized by pea diamine oxidase. Copyright (C) 1997 Elsevier Science Ltd.

引用

页码：997 / 1000

页数：4

共 15 条

[1] DIAMINE OXIDASE FROM MILLET CATALYZES THE OXIDATION OF 1,3-DIAMINOPROPANE [J].