Information on EC 1.21.4.3 - sarcosine reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.21.4.3
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RECOMMENDED NAME
GeneOntology No.
sarcosine reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl phosphate + methylamine + thioredoxin disulfide + H2O = N-methylglycine + phosphate + thioredoxin
show the reaction diagram
The reaction is observed only in the direction of sarcosine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for sarcosine binding and methylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.4 (betaine reductase)
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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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SYSTEMATIC NAME
IUBMB Comments
acetyl-phosphate methylamine:thioredoxin disulfide oxidoreductase (N-methylglycine-forming)
The reaction is observed only in the direction of sarcosine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for sarcosine binding and methylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.4 (betaine reductase).
CAS REGISTRY NUMBER
COMMENTARY hide
125752-88-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 87, ATCC 12837
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Manually annotated by BRENDA team
DSM 402
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-
Manually annotated by BRENDA team
DSM 525, ATCC 6013
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-
Manually annotated by BRENDA team
DSM 633
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-
Manually annotated by BRENDA team
DSM 6911, grown on creatine
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-methylglycine + phosphate + dithioerythritol
acetyl phosphate + methylamine + dithioerythritol disulfide
show the reaction diagram
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-
-
?
N-methylglycine + phosphate + thioredoxin
acetyl phosphate + methylamine + thioredoxin disulfide
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
N-methylglycine + phosphate + thioredoxin
acetyl phosphate + methylamine + thioredoxin disulfide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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5% of activity compared to NADPH
NADPH
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preferred as physiological electron donor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
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can serve as artificial electron donor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
dithioerythritol
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pH 7.7, 37C
3.7
N-methylglycine
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pH 7.7, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
114
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pH 7, 37C, extract from bacteria that were grown on alanine and sarcosine
137
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pH 7.7, 37C, extract from bacteria that were grown on formate and creatine
217
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pH 7.7, 37C, extract from bacteria that were grown on formate and sarcosine
229
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pH 7, 37C, extract from bacteria that were grown on formate and sarcosine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 8
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highest activity in K-phosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
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protein A, SDS-PAGE
45000
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protein A, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 21000, gel filtration, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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complete loss of activity within 24 h
636282
5.2
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38% loss of activity within 24 h
636282
5.4 - 5.8
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10% loss of activity within 24 h
636282
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 15% loss of activity within one week
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-20C, stable for several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
components A, B and C of enzyme complex purified separately
Show AA Sequence (204 entries)
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