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A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans.
Nature. 2001 Mar 22; 410(6827):490-4.Nat

Abstract

Considerable evidence indicates that NO biology involves a family of NO-related molecules and that S-nitrosothiols (SNOs) are central to signal transduction and host defence. It is unknown, however, how cells switch off the signals or protect themselves from the SNOs produced for defence purposes. Here we have purified a single activity from Escherichia coli, Saccharomyces cerevisiae and mouse macrophages that metabolizes S-nitrosoglutathione (GSNO), and show that it is the glutathione-dependent formaldehyde dehydrogenase. Although the enzyme is highly specific for GSNO, it controls intracellular levels of both GSNO and S-nitrosylated proteins. Such 'GSNO reductase' activity is widely distributed in mammals. Deleting the reductase gene in yeast and mice abolishes the GSNO-consuming activity, and increases the cellular quantity of both GSNO and protein SNO. Furthermore, mutant yeast cells show increased susceptibility to a nitrosative challenge, whereas their resistance to oxidative stress is unimpaired. We conclude that GSNO reductase is evolutionarily conserved from bacteria to humans, is critical for SNO homeostasis, and protects against nitrosative stress.

Authors+Show Affiliations

Howard Hughes Medical Institute, Duke Medical Center, North Carolina 27710, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

11260719

Citation

Liu, L, et al. "A Metabolic Enzyme for S-nitrosothiol Conserved From Bacteria to Humans." Nature, vol. 410, no. 6827, 2001, pp. 490-4.
Liu L, Hausladen A, Zeng M, et al. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature. 2001;410(6827):490-4.
Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., & Stamler, J. S. (2001). A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature, 410(6827), 490-4.
Liu L, et al. A Metabolic Enzyme for S-nitrosothiol Conserved From Bacteria to Humans. Nature. 2001 Mar 22;410(6827):490-4. PubMed PMID: 11260719.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. AU - Liu,L, AU - Hausladen,A, AU - Zeng,M, AU - Que,L, AU - Heitman,J, AU - Stamler,J S, PY - 2001/3/22/pubmed PY - 2001/4/21/medline PY - 2001/3/22/entrez SP - 490 EP - 4 JF - Nature JO - Nature VL - 410 IS - 6827 N2 - Considerable evidence indicates that NO biology involves a family of NO-related molecules and that S-nitrosothiols (SNOs) are central to signal transduction and host defence. It is unknown, however, how cells switch off the signals or protect themselves from the SNOs produced for defence purposes. Here we have purified a single activity from Escherichia coli, Saccharomyces cerevisiae and mouse macrophages that metabolizes S-nitrosoglutathione (GSNO), and show that it is the glutathione-dependent formaldehyde dehydrogenase. Although the enzyme is highly specific for GSNO, it controls intracellular levels of both GSNO and S-nitrosylated proteins. Such 'GSNO reductase' activity is widely distributed in mammals. Deleting the reductase gene in yeast and mice abolishes the GSNO-consuming activity, and increases the cellular quantity of both GSNO and protein SNO. Furthermore, mutant yeast cells show increased susceptibility to a nitrosative challenge, whereas their resistance to oxidative stress is unimpaired. We conclude that GSNO reductase is evolutionarily conserved from bacteria to humans, is critical for SNO homeostasis, and protects against nitrosative stress. SN - 0028-0836 UR - https://www.unboundmedicine.com/medline/citation/11260719/A_metabolic_enzyme_for_S_nitrosothiol_conserved_from_bacteria_to_humans_ L2 - https://doi.org/10.1038/35068596 DB - PRIME DP - Unbound Medicine ER -