Information on EC 1.3.8.13 - crotonobetainyl-CoA reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.8.13
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RECOMMENDED NAME
GeneOntology No.
crotonobetainyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
gamma-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-carnitine degradation I
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SYSTEMATIC NAME
IUBMB Comments
gamma-butyrobetainyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21, L-carnitine CoA-transferase. The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonobetaine + reduced benzylviologen
gamma-butyrobetaine + oxidized benzylviologen
show the reaction diagram
crotonobetainyl-CoA + reduced benzylviologen
gamma-butyrobetainyl-CoA + oxidized benzylviologen
show the reaction diagram
crotonobetainyl-CoA + reduced electron-transfer flavoprotein
gamma-butyrobetainyl-CoA + electron-transfer flavoprotein
show the reaction diagram
gamma-butyrobetainyl-CoA + electron-transfer flavoprotein
crotonobetainyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
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?
additional information
?
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presence of L-carnitine dehydratase is required for enzymatic activity
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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
crotonobetainyl-CoA + reduced electron-transfer flavoprotein
gamma-butyrobetainyl-CoA + electron-transfer flavoprotein
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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contains non-covalently bound FAD in a molar ratio of 1:1
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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6.6 mM, 48% inhibition
choline
Cu2+
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1 mM, 100% inhibition
D-carnitine
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D-glucose
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350 mM, complete loss of activity
dithioerythritol
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6.6 mM, 85% inhibition
EDTA
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3.3 mM, 32% inhibition
Fe2+
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1 mM, 94% inhibition
gamma-butyrobetaine
glutathione
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6.6 mM, 67% inhibition
Hg2+
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1 mM, 97% inhibition
Tris-HCl
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Zn2+
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1 mM, 58% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.7
crotonobetaine
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pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
gamma-butyrobetaine
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pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.35
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pH not specified in the publication, temperature not specified in the publication
233
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pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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potassium phosphate buffer
additional information
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Tris-HCl buffer is inhibitory
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 45
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41500
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4 * 41500, SDS-PAGE
41800
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164400
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gel filtration
166000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
crotonobetaine and L-carnitine induce enzymes of carnitine metabolism
fumarate causes a stimulation of growth and an increased expression of crotonobetaine reductase
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gamma-butyrobetaie and glucose repress carnitine metabolism
inducible enzyme detectable only in cells grown anaerobically in the presence of L-carnitine or crotonobetaine as inducers
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Show AA Sequence (367 entries)
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