Information on EC 1.1.1.306 - S-(hydroxymethyl)mycothiol dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.306
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RECOMMENDED NAME
GeneOntology No.
S-(hydroxymethyl)mycothiol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-(hydroxymethyl)mycothiol + NAD+ = S-formylmycothiol + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde oxidation III (mycothiol-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.
CAS REGISTRY NUMBER
COMMENTARY hide
192140-85-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain mc2
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Manually annotated by BRENDA team
strain mc2
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Manually annotated by BRENDA team
strain NRRL 5646
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Manually annotated by BRENDA team
strain NRRL 5646
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-butanol + NAD+
n-butanal + NADH
show the reaction diagram
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-
-
?
12-hydroxydodecanoic acid + NADH
? + NAD+
show the reaction diagram
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?
formaldehyde + 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol + NAD+
S-formylmycothiol + NADH
show the reaction diagram
mycothiol + NAD+
? + NADH + H+
show the reaction diagram
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
show the reaction diagram
S-hydroxymethylmycothiol + NAD+
formic acid + mycothiol + NADH + ?
show the reaction diagram
S-nitrosomycothiol + NADH
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
S-(hydroxymethyl)mycothiol + NAD+
S-formylmycothiol + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-myo-inositol
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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6 atoms Zn/enzyme molecule
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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80% inhibition at 5 mM
2-(cyclohexylamino)ethanesulfonic acid-NaOH
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25 mM at pH 9.0: 80% of the activity compared to 0.1 M diphosphate, pH 9.0
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acetaldehyde
Cu2+
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complete inhibition at 1 mM
Glycine-NaOH
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100 mM at pH 9.0: 40% of the activity compared to 0.1 M diphosphate, pH 9.0
Hg2+
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complete inhibition at 0.1 mM
KCN
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55% inhibition at 2 mM
Na2B4O7-HCl
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100 mM at pH 9.0: no activity
Tris-HCl
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50 mM at pH 9.0: 80% of the activity compared to 0.1 M diphosphate, pH 9.0
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
factor
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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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formaldehyde
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methanol
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can replace an unidentified activating factor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
1-Hexanol
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1.2
1-Octanol
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26.5
1-Pentanol
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324
1-propanol
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1.7
12-Hydroxydodecanoic acid
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9.6
formaldehyde
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0.0173
mycothiol
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pH 8.7, 30°C
0.354
NAD+
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pH 8.7, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Mycobacterium smegmatis
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
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cell free extract, in the absence of an unknown activating factor
0.08
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cell free extract, in the presence of an unknown activating factor
6.9
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substrate: ethanol
15
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substrate: formaldehyde
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9.5
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optimal in Na-diphosphate buffer, buffers containing amino groups give poor activity, possibly because of Schiff base formation with formaldehyde
9
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formaldehyde as substrate
10.2
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alcohols as substrates
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38263
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x * 38263, electrospray mass spectrometry
40000
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3 * 40000, SDS-PAGE
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
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3 * 40000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mFADH genetic organization, overview
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (370 entries)
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