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1.1.1.284: S-(hydroxymethyl)glutathione dehydrogenase

This is an abbreviated version!
For detailed information about S-(hydroxymethyl)glutathione dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.284

Reaction

S-(hydroxymethyl)glutathione
+
NAD(P)+
=
S-formylglutathione
+
NAD(P)H
+
H+

Synonyms

ADH III, ADH3, ADH4, ADH5, AdhC, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase class III, alcohol dehydrogenase class-3, Alcohol dehydrogenase SFA, AN7632.2, AtGSNOR, c-ADH, carbonyl reductase 1, CBR1, class III ADH, class III alcohol dehydrogenase, dehydrogenase, formaldehyde, EC 1.2.1.1, FALDH, FDH, FLD, FldA, formaldehyde dehydrogenase, formaldehyde dehydrogenase (glutathione), formic dehydrogenase, FrxA, GD-FAlDH, GFD, glutathione (GSH)-dependent formaldehyde dehydrogenase, glutathione-dependent alcohol dehydrogenase, Glutathione-dependent formaldehyde dehydrogenase, GS-FDH, GSH-FDH, GSNO reductase, GSNO-R, GSNOR, GSNOR1, HMGSH dehydrogenase, HOT5, MGG_06011, NAD- and glutathione-dependent formaldehyde dehydrogenase, NAD-dependent formaldehyde dehydrogenase, NAD-linked formaldehyde dehydrogenase, NADH-GSNO oxidoreductase, nitroreductase, NTRA, Os02g0815500, Os02G57040, OsGSNOR, PmFLD1, PmGSNOR, S-nitrosoglutathione reductase, SA0UHSC_00833, SFA1, SlGSNOR, SoGSNOR, Tc-GFD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.284 S-(hydroxymethyl)glutathione dehydrogenase

Posttranslational Modification

Posttranslational Modification on EC 1.1.1.284 - S-(hydroxymethyl)glutathione dehydrogenase

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrosylation
S-nitrosylation
the not Zn2+ chelating cysteine residues Cys10, Cys271 and Cys370 of Arabidopsis are targets for S-nitrosylation. Whereas modification of Cys370 seems to promote Snitrosylation of Cys10 and Cys271 by inducing conformational changes that alters the solvent accessibility and electrostatic environment of these cysteine residues. In detail, Snitrosylation of GSNOR slightly changes the solvent accessibility of amino acids from the substrate binding site and/or the dimer interface. Mass spectrometric analysis confirms the presence of monomeric and dimeric S-nitrosylated GSNOR, while unmodified GSNOR exists as dimers