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Information on EC 1.1.1.306 - S-(hydroxymethyl)mycothiol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.306
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.306 S-(hydroxymethyl)mycothiol dehydrogenase
IUBMB Comments
S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.1.1.306
- methanol
- acetaldehyde
- dehydrogenases
- actinomycetes
-
methylotrophic
- erythropolis
-
nad-linked
-
corynebacterium
-
zinc-containing
-
rhodococcus
- glutamicum
showSynonyms
mycothiol-dependent formaldehyde dehydrogenase, fd-fa1dh, mfadh, msh-dependent formaldehyde dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.2.1.66
-
-
formerly
-
glutathione-independent formaldehyde dehydrogenase
-
-
-
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MD-FALDH
-
-
-
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mFADH
MSH-dependent formaldehyde dehydrogenase
mycothiol-dependent formaldehyde dehydrogenase
NAD/factor-dependent formaldehyde dehydrogenase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-(hydroxymethyl)mycothiol + NAD+ = S-formylmycothiol + NADH + H+
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
formaldehyde oxidation III (mycothiol-dependent), formaldehyde oxidation V (bacillithiol-dependent)
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SYSTEMATIC NAME
IUBMB Comments
S-(hydroxymethyl)mycothiol:NAD+ oxidoreductase
S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
192140-85-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-pentanol + NAD+
pentanal + NADH + H+
-
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
-
Substrates: -
Products: -
Products: -
r
12-hydroxydodecanoic acid + NADH
? + NAD+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
-
Substrates: -
Products: -
Products: -
?
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
-
Substrates: -
Products: -
Products: -
?
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
-
Substrates: -
Products: -
Products: -
?
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
-
Substrates: -
Products: -
Products: -
?
S-hydroxymethylmycothiol + NAD+
formic acid + mycothiol + NADH + ?
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Substrates: rapid-equilibrium ordered mechanism
Products: -
Products: -
?
S-hydroxymethylmycothiol + NAD+
formic acid + mycothiol + NADH + ?
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Substrates: rapid-equilibrium ordered mechanism
Products: -
Products: -
?
S-nitrosomycothiol + NADH
?
-
Substrates: decomposition with a sequential mechanism, enzyme reduces the nitroso group to the oxidation level of nitroxyl
Products: -
Products: -
?
S-nitrosomycothiol + NADH
?
-
Substrates: decomposition with a sequential mechanism, enzyme reduces the nitroso group to the oxidation level of nitroxyl
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
-
Substrates: -
Products: -
Products: -
?
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
-
Substrates: -
Products: -
Products: -
?
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
-
Substrates: -
Products: -
Products: -
?
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
-
mycothiol
1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
-
mycothiol
1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
-
high specificity for mycothiol
1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
-
high specificity for mycothiol
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(cyclohexylamino)ethanesulfonic acid-NaOH
-
25 mM at pH 9.0: 80% of the activity compared to 0.1 M diphosphate, pH 9.0
glycine-NaOH
-
100 mM at pH 9.0: 40% of the activity compared to 0.1 M diphosphate, pH 9.0
Tris-HCl
-
50 mM at pH 9.0: 80% of the activity compared to 0.1 M diphosphate, pH 9.0
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
factor
-
unidentified factor that is required for maximal activity with formaldehyde as substrate, only 4% activity in its absence, oxidation of alcohols do not require the factor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
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cell free extract, in the absence of an unknown activating factor
0.08
-
cell free extract, in the presence of an unknown activating factor
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9.5
-
optimal in Na-diphosphate buffer, buffers containing amino groups give poor activity, possibly because of Schiff base formation with formaldehyde
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
induction of enzyme and factor synthesis only if cells grown in methanol-containing medium
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the organism has three distinct formaldehyde oxidation systems, the methlotrophhic oxidoreductase mycothiol-dependent formaldehyde dehydroganse is not a key enzyme invovled in oligotrophic growth
metabolism
-
the organism has three distinct formaldehyde oxidation systems, the methlotrophhic oxidoreductase mycothiol-dependent formaldehyde dehydroganse is not a key enzyme invovled in oligotrophic growth
-
Show AA Sequence and Transmembrane Helices (2223 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
formaldehyde, added to the medium, induces the enzyme expression by 10fold
the gene encoding the enzyme is not induced under oligotrophic conditions
formaldehyde, added to the medium, induces the enzyme expression by 10fold
-
formaldehyde, added to the medium, induces the enzyme expression by 10fold
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-
the gene encoding the enzyme is not induced under oligotrophic conditions
-
the gene encoding the enzyme is not induced under oligotrophic conditions
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-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
thiol formation and detection of MSH-dependent formaldehyde dehydrogenase activity in cell extracts are relevant to the possible modulation of nitric oxide toxicity generated by strain NRRL 5646
additional information
-
thiol formation and detection of MSH-dependent formaldehyde dehydrogenase activity in cell extracts are relevant to the possible modulation of nitric oxide toxicity generated by strain NRRL 5646
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Misset-Smits, M.; van Ophem, P.W.; Sakuda, S.; Duine, J.A.
Mycothiol, 1-O-(2'-[N-acwtyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase
FEBS Lett.
409
221-222
1997
Amycolatopsis methanolica, Rhodococcus erythropolis
brenda
Norin, A.; van Ophem, P.W.; Piersma, S.R.; Persson, B.; Duine, J.A.; Jrnvall, H.
Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaroytic alcohol dehydrogenases. Primary structure, conformational modelling and functional correlations
Eur. J. Biochem.
248
282-289
1997
Amycolatopsis methanolica
brenda
Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A.
NAD-linked, factor-dependent formaldehyde dehydrogenase or trimeric, zinc-containing, long-chain alcohol dehydrogenase from Amycolatopsis methanolica
Eur. J. Biochem.
206
511-518
1992
Amycolatopsis methanolica
brenda
Vogt, R.N.; Steenkamp, D.J.; Zheng, R.; Blanchard, J.S.
The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase
Biochem. J.
374
657-666
2003
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2
brenda
Lee, S.; Bergeron, H.; Lau, P.C.; Rosazza, J.P.
Thiols in nitric oxide synthase-containing Nocardia sp. strain NRRL 5646
Appl. Environ. Microbiol.
73
3095-3097
2007
Nocardia sp., Nocardia sp. NRRL 5646
brenda
Yoshida, N.; Hayasaki, T.; Takagi, H.
Gene expression analysis of methylotrophic oxidoreductases involved in the oligotrophic growth of Rhodococcus erythropolis N9T-4
Biosci. Biotechnol. Biochem.
75
123-127
2011
Rhodococcus erythropolis, Rhodococcus erythropolis N9T-4
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.306)
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Release 2023.1 (January 2023)
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