S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

M. R. Fernández; J. A. Biosca; X. Parés

doi:https://doi.org/10.1007/s00018-003-3025-x

S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

M. R. Fernández, J. A. Biosca, X. Parés

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

39 Citations (Scopus)

Abstract

S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM-1 min-1, respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 μM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.

Original language	English
Pages (from-to)	1013-1018
Journal	Cellular and Molecular Life Sciences
Volume	60
DOIs	https://doi.org/10.1007/s00018-003-3025-x
Publication status	Published - 1 May 2003

Keywords

ADH3
Alcohol dehydrogenase
Formaldehyde dehydrogenase
Nitrosative stress
Nitrosoglutathione
Nuclear enzyme

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title = "S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation",

abstract = "S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM-1 min-1, respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 μM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.",

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TY - JOUR

T1 - S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

AU - Fernández, M. R.

AU - Biosca, J. A.

AU - Parés, X.

PY - 2003/5/1

Y1 - 2003/5/1

N2 - S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM-1 min-1, respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 μM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.

AB - S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM-1 min-1, respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 μM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.

KW - ADH3

KW - Alcohol dehydrogenase

KW - Formaldehyde dehydrogenase

KW - Nitrosative stress

KW - Nitrosoglutathione

KW - Nuclear enzyme

U2 - https://doi.org/10.1007/s00018-003-3025-x

DO - https://doi.org/10.1007/s00018-003-3025-x

M3 - Article

VL - 60

SP - 1013

EP - 1018

ER -

S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

Abstract

Keywords

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