Information on EC 4.2.1.149 - crotonobetainyl-CoA hydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.149
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RECOMMENDED NAME
GeneOntology No.
crotonobetainyl-CoA hydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-carnitine degradation I
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carnitine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-carnitinyl-CoA hydro-lyase [(E)-4-(trimethylammonio)but-2-enoyl-CoA-forming]
The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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SwissProt
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
(E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
L-carnitinyl-CoA
show the reaction diagram
crotonobetainyl-CoA + H2O
L-carnitinyl-CoA
show the reaction diagram
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-
-
r
crotonyl-CoA + H2O
?
show the reaction diagram
L-carnitinyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
show the reaction diagram
L-carnitinyl-CoA
crotonobetainyl-CoA + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
does not use crotonobetaine as substrate
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-
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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
(E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
L-carnitinyl-CoA
show the reaction diagram
crotonobetainyl-CoA + H2O
L-carnitinyl-CoA
show the reaction diagram
P31551
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-
-
r
crotonyl-CoA + H2O
?
show the reaction diagram
P31551
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-
-
?
L-carnitinyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
show the reaction diagram
L-carnitinyl-CoA
crotonobetainyl-CoA + H2O
show the reaction diagram
P31551
-
-
-
r
additional information
?
-
P31551
does not use crotonobetaine as substrate
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-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetoacetyl-CoA
0.1 mM, 25% inhibition
acetyl-CoA
0.1 mM, 23% inhibition
butyryl-CoA
0.1 mM, 29% inhibition
CoA
0.1 mM, 29% inhibition
decanoyl-CoA
0.1 mM, 79% inhibition
gamma-butyrobetainyl-CoA
0.1 mM, 27% inhibition, competitive inhibitor
Hexanoyl-CoA
0.1 mM, 43% inhibition
palmitoyl-CoA
0.01 mM, 87% inhibition
succinyl-CoA
0.1 mM, 22% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
(E)-4-(trimethylammonio)but-2-enoyl-CoA
37C, pH 7.5
0.012
crotonobetainyl-CoA
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at pH 7.5 and 37C
0.038 - 0.52
crotonyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068
gamma-butyrobetainyl-CoA
37C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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cell free extract, in 10 mM sodium phosphate buffer (pH 7.8), at 37C
60.3
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cell-free extract, at pH 7.5 and 37C
450
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after 150fold purification, in 10 mM sodium phosphate buffer (pH 7.8), at 37C
699.9
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after 11.6fold purification, at pH 7.5 and 37C
6088
37C, pH 7.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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calculated from amino acid sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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x * 27000, SDS-PAGE
32329
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x * 32329, calculated from amino acid sequence
40000
3 * 40000, SDS-PAGE
43600
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2 * 43600, SDS-PAGE
84200
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gel filtration
85700
gel filtration
87000
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gel filtration
91100
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calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 43600, SDS-PAGE
homotrimer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0 or 20C, purified enzyme in 50 mM sodium phosphate buffer containing 150 mM NaCl, 48 h, complete loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Resource Q column chromatography, and Superose 12HR gel filtration
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DEAE-Sepharose column chromatography and Resource Q column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strain K38
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Show AA Sequence (446 entries)
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