NITRIC-OXIDE AND NAD-DEPENDENT PROTEIN MODIFICATION

被引：24

作者：

MCDONALD, LJ

MOSS, J

机构：

[1] Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, 20892, MD

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1994年 / 138卷 / 1-2期

关键词：

NITRIC OXIDE; NAD; ADP-RIBOSYLATION; CYSTEINE;

D O I：

10.1007/BF00928462

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Nitric oxide (NO) has been suggested to act as a regulator of endogenous intracellular ADP-ribosylation, based on radiolabelling of proteins in tissue homogenates incubated with [P-32]NAD and NO. After the NO-stimulated modification was replicated in a defined system containing only the purified acceptor protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the hypothesis of NO-stimulation of an endogenous ADP-ribosyltransferase became moot. The NO-stimulated, NAD-dependent modification of GAPDH was recently characterized as covalent binding of the whole NAD molecule to the enzyme, not ADP-ribosylation. With this result, along with the knowledge that GAPDH is stoichiometrically S-nitrosylated, the role of NO in protein modification with NAD may be viewed as the conferring of an unexpected chemical reactivity upon GAPDH, possibly due to nitrosylation of a cysteine in the enzyme active site.

引用

页码：201 / 206

页数：6

共 44 条

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