Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa

被引：10

作者：

Cho, YS

Han, MK

Kwark, OS

Phoe, MS

Cha, YS

An, NH

Kim, UH ^{[1
]}

机构：

[1] Chonbuk Natl Univ, Sch Med, Dept Biochem, Chonju 561182, South Korea

[2] Chonbuk Natl Univ, Sch Med, Inst Cardiovasc Res, Chonju 561182, South Korea

[3] Wonkwang Univ, Coll Pharm, Iksan 570749, South Korea

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1998年 / 120卷 / 01期

关键词：

NADase; ADP-ribosylation; self-inactivation; NAD; Neurospora crassa; purification; mycelia; cysteine;

D O I：

10.1016/S0305-0491(98)10006-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

NAD glycohydrolase (NADase; EC 3.2.2.5) is an enzyme that catalyzes hydrolysis of NAD to produce ADP-ribose and nicotinamide. We recently demonstrated that self-inactivation of NADase from rabbit erythrocytes was due to an auto-ADP-ribosylation. In the present study, a mechanism of self-inactivation of NADase from Neurospora crassa by its substrate was investigated by using intact mycelia of N. crassa and purified NADase, which had molecular characteristics different from mammalian NADases, The results suggested that inactivation of NADase from N. crassa was also due to an auto-ADP-ribosylation. These findings indicate that the auto-modification of NADase is one of the universal phenomena to regulate enzyme functions. (C) 1998 Elsevier Science Inc. All rights reserved.

引用

页码：175 / 181

页数：7

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