Any feedback?
Information on EC 1.3.1.85 - crotonyl-CoA carboxylase/reductase
for references in articles please use BRENDA:EC1.3.1.85Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.3.1.85 crotonyl-CoA carboxylase/reductaseIUBMB Comments
The reaction is catalysed in the reverse direction. This enzyme, isolated from the bacterium Rhodobacter sphaeroides, catalyses (E)-but-2-enoyl-CoA-dependent oxidation of NADPH in the presence of CO2. When CO2 is absent, the enzyme catalyses the reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA, but with only 10% of maximal activity (relative to (E)-but-2-enoyl-CoA carboxylation).
Specify your search results
Word Map
- 1.3.1.85
- polyketide
-
rhodobacter
- acyl-coas
- glyoxylate
- sphaeroides
- propionyl-coa
- 3-hydroxypropionate
- extorquens
-
methylobacterium
- butyryl-coa
The enzyme appears in viruses and cellular organisms
Synonyms
crotonyl-coa carboxylase/reductase, 2-octenoyl-coa carboxylase/reductase, enoyl-coa carboxylase/reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AntE
CCR
CCR1
CCRC
crotonyl-CoA carboxylase/reductase
crotonyl-CoA reductase (carboxylating)
-
-
-
-
crotonyl-CoA reductase-carboxylase
ECR
enoyl-CoA carboxylase/reductase
CCR
-
-
ambiguous
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-ethylmalonyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + CO2 + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
reductive carboxylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
-
,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(2S)-ethylmalonyl-CoA:NADP+ oxidoreductase (decarboxylating)
The reaction is catalysed in the reverse direction. This enzyme, isolated from the bacterium Rhodobacter sphaeroides, catalyses (E)-but-2-enoyl-CoA-dependent oxidation of NADPH in the presence of CO2. When CO2 is absent, the enzyme catalyses the reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA, but with only 10% of maximal activity (relative to (E)-but-2-enoyl-CoA carboxylation).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-3-cyclohexylprop-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-3-cyclohexylpropanoyl-CoA + NADP+
(2E)-4-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
[(2R)-2-methylbutyl]propanedioyl-CoA + NADP+
(2E)-5-chloropent-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-5-chloropentanoyl-CoA + NADP+
(2E)-5-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-(3-methylbutyl)propanedioyl-CoA + NADP+
(2E)-6-methyloct-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-6-methyloctanoyl-CoA + NADP+
-
-
-
?
(2E)-hept-2-en-6-ynoyl-CoA + NADPH + CO2 + H+
(2S)-2-craboxy-hept-6-ynoyl-CoA + NADP+
-
-
-
?
(2E)-hex-2-enoyl-CoA + NADPH + CO2 + H+
(S)-2-butylpropanedioyl-CoA + NADP+
-
-
-
?
(E)-crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
100% relative specific activity, the carboxylation reaction is the physiologically relevant reaction
-
-
r
(E)-crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
10% of maximal activity (compared with vmax of crotonyl-CoA carboxylation)
-
-
?
acryloyl-CoA + CO2 + NADPH + H+
methylmalonyl-CoA + NADP+
-
acryloyl-CoA is accepted as an alternative substrate analogue by the enzyme with 40% relative activity (compared with vmax of crotonyl-CoA carboxylation)
-
-
?
(2E)-3-cyclohexylprop-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-3-cyclohexylpropanoyl-CoA + NADP+
-
-
-
?
(2E)-3-cyclohexylprop-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-3-cyclohexylpropanoyl-CoA + NADP+
-
-
-
?
(2E)-4-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
[(2R)-2-methylbutyl]propanedioyl-CoA + NADP+
-
-
-
?
(2E)-4-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
[(2R)-2-methylbutyl]propanedioyl-CoA + NADP+
-
-
-
?
(2E)-5-chloropent-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-5-chloropentanoyl-CoA + NADP+
-
-
-
?
(2E)-5-chloropent-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxy-5-chloropentanoyl-CoA + NADP+
-
-
-
?
(2E)-5-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-(3-methylbutyl)propanedioyl-CoA + NADP+
-
-
-
?
(2E)-5-methylhex-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-(3-methylbutyl)propanedioyl-CoA + NADP+
-
-
-
?
(2E)-oct-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxyoctanoyl-CoA + NADP+
-
-
-
-
?
(2E)-oct-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxyoctanoyl-CoA + NADP+
-
-
-
-
?
(2E)-oct-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxyoctanoyl-CoA + NADP+
-
-
-
?
3-indolylacryloyl-CoA + NADPH + CO2 + H+
indolylmethylmalonyl-CoA + NADP+
-
-
-
?
3-indolylacryloyl-CoA + NADPH + CO2 + H+
indolylmethylmalonyl-CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-(4-hydroxyphenyl)propionyl-CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-(4-hydroxyphenyl)propionyl-CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-phenylpropionyl-CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-phenylpropionyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
crotonyl-CoA is the best substrate
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
crotonyl-CoA is the best substrate
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
crotonyl-CoA is the best substrate
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NADPH + CO2 + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NADPH + CO2 + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
reduction at low rate
-
-
ir
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
reduction at low rate
-
-
ir
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
reduction at low rate
-
-
ir
additional information
?
-
-
does not reduce crotonyl-N-acetylcysteamine, methacryloyl-CoA, 6-hydroxycylohex-1-ene-1-carboxyl-CoA, cyclo-hexa-1,5-diene-1-carboxyl-CoA, acetoacetyl-CoA, propionyl-CoA, (R)-3-hydroxybutyryl-CoA, (S)-3-hydroxybutyryl-CoA (less than 1% specific activity)
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reduction of crotonyl-CoA to butyryl-CoA in the absence of CO2, but with only about one tenth of the maximum rate
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of crotonyl-CoA to butyryl-CoA as a side reaction, but only in the absence of CO2 and at low catalytic efficiency
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of crotonyl-CoA to butyryl-CoA as a side reaction, but only in the absence of CO2 and at low catalytic efficiency
-
-
-
additional information
?
-
-
the enzyme also catalyzes the reduction of crotonyl-CoA to butyryl-CoA in the absence of CO2, but with only about one tenth of the maximum rate
-
-
?
additional information
?
-
-
the enzyme also catalyzes the reduction of crotonyl-CoA to butyryl-CoA in the absence of CO2, but with only about one tenth of the maximum rate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
100% relative specific activity, the carboxylation reaction is the physiologically relevant reaction
-
-
r
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comprehensive metal analysis of crotonyl-CoA carboxylase/reductase by plasma emission spectroscopy indicates the absence of any metals
additional information
-
comprehensive metal analysis of crotonyl-CoA carboxylase/reductase by plasma emission spectroscopy indicates the absence of any metals
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetate
B8XVS5
activity is upregulated during photoheterotrophic growth on acetate compared to the activities during growth on succinate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
(2S)-ethylmalonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.5
acryloyl-CoA
-
pH and temperature not specified in the publication
0.2
(E)-crotonyl-CoA
-
for reduction, pH and temperature not specified in the publication
0.4
(E)-crotonyl-CoA
-
for reductive carboxylation, pH and temperature not specified in the publication
0.14
4-coumaroyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
0.2
4-coumaroyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.089
cinnamoyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.38
cinnamoyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.2
CO2
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.4
crotonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.49
crotonyl-CoA
mutant enzyme V350F, pH and temperature not specified in the publication
1.17
crotonyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
1.21
crotonyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
1.31
crotonyl-CoA
mutant enzyme A182L, pH and temperature not specified in the publication
1.58
crotonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.7
NADPH
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
104
(2S)-ethylmalonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.0735
4-coumaroyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
0.109
4-coumaroyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.0688
cinnamoyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.0877
cinnamoyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.0675
crotonyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.1197
crotonyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
0.1263
crotonyl-CoA
mutant enzyme V350F, pH and temperature not specified in the publication
0.1519
crotonyl-CoA
mutant enzyme A182L, pH and temperature not specified in the publication
0.1755
crotonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
520
(2S)-ethylmalonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.525
4-coumaroyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
0.545
4-coumaroyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.18
cinnamoyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.985
cinnamoyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.0583
crotonyl-CoA
mutant enzyme V350G, pH and temperature not specified in the publication
0.111
crotonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.115
crotonyl-CoA
mutant enzyme A182L, pH and temperature not specified in the publication
0.257
crotonyl-CoA
mutant enzyme V350A, pH and temperature not specified in the publication
0.257
crotonyl-CoA
mutant enzyme V350F, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
