Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa

Yee Sook Cho; Myung Kwan Han; Ok Sun Kwark; Moon Sik Phoe; Youn Soo Cha; Nyeon Hyoung An; Uh Hyun Kim

doi:10.1016/S0305-0491(98)10006-8

Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa

Yee Sook Cho
, Myung Kwan Han
, Ok Sun Kwark
, Moon Sik Phoe
, Youn Soo Cha
, Nyeon Hyoung An
, Uh Hyun Kim^*

^*Corresponding author for this work

Department of Medicine

Jeonbuk National University
Chonnam National University
Wonkwang University

Research output: Contribution to journal › Journal article › peer-review

11 Scopus citations

Abstract

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. Copyright (C) 1998 Elsevier Science Inc.

Original language	English
Pages (from-to)	175-181
Number of pages	7
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	120
Issue number	1
DOIs	https://doi.org/10.1016/S0305-0491(98)10006-8
State	Published - 1998

Keywords

ADP-ribosylation
Cysteine
Mycelia
NAD
NADase
Neurospora crassa
Purification
Self-inactivation

Quacquarelli Symonds(QS) Subject Topics

Agriculture & Forestry
Anatomy & Physiology
Biological Sciences

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10.1016/S0305-0491(98)10006-8

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@article{56ddf46d19864553b1b6ad6d67a34bdc,

title = "Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa",

abstract = "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. Copyright (C) 1998 Elsevier Science Inc.",

keywords = "ADP-ribosylation, Cysteine, Mycelia, NAD, NADase, Neurospora crassa, Purification, Self-inactivation",

author = "Cho, \{Yee Sook\} and Han, \{Myung Kwan\} and Kwark, \{Ok Sun\} and Phoe, \{Moon Sik\} and Cha, \{Youn Soo\} and An, \{Nyeon Hyoung\} and Kim, \{Uh Hyun\}",

year = "1998",

doi = "10.1016/S0305-0491(98)10006-8",

language = "English",

volume = "120",

pages = "175--181",

journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",

issn = "0305-0491",

number = "1",

}

TY - JOUR

T1 - Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa

AU - Cho, Yee Sook

AU - Han, Myung Kwan

AU - Kwark, Ok Sun

AU - Phoe, Moon Sik

AU - Cha, Youn Soo

AU - An, Nyeon Hyoung

AU - Kim, Uh Hyun

PY - 1998

Y1 - 1998

N2 - 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. Copyright (C) 1998 Elsevier Science Inc.

AB - 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. Copyright (C) 1998 Elsevier Science Inc.

KW - ADP-ribosylation

KW - Cysteine

KW - Mycelia

KW - NAD

KW - NADase

KW - Neurospora crassa

KW - Purification

KW - Self-inactivation

UR - https://www.scopus.com/pages/publications/0031874902

U2 - 10.1016/S0305-0491(98)10006-8

DO - 10.1016/S0305-0491(98)10006-8

M3 - Journal article

C2 - 9787786

AN - SCOPUS:0031874902

SN - 0305-0491

VL - 120

SP - 175

EP - 181

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

IS - 1

ER -

Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa

Abstract

Keywords

Quacquarelli Symonds(QS) Subject Topics

Access to Document

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