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(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+
-
-
-
?
(2E)-oct-2-enoyl-CoA + NADPH + CO2 + H+
(2S)-2-carboxyoctanoyl-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)
-
-
?
3-indolylacryloyl-CoA + NADPH + CO2 + H+
indolylmethylmalonyl-CoA + NADP+
4-coumaroyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-(4-hydroxyphenyl)propionyl-CoA + NADP+
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)
-
-
?
cinnamoyl-CoA + NADPH + CO2 + H+
(2S)2-carboxy-3-phenylpropionyl-CoA + NADP+
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
crotonyl-CoA + CO2 + NADPH + H+
?
crotonyl-CoA + NADPH + CO2 + H+
(2S)-ethylmalonyl-CoA + NADP+
crotonyl-CoA + NADPH + H+
?
-
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
decanoyl-CoA + NADPH + H+
?
-
-
-
?
hexanoyl-CoA + NADPH + H+
?
-
-
-
?
octanoyl-CoA + NADPH + H+
?
-
-
-
?
additional information
?
-
(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 + CO2 + NADPH + H+
?
-
-
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
?
-
-
-
-
?
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
-
-
?
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0.2
(2S)-ethylmalonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.2 - 0.4
(E)-crotonyl-CoA
0.14 - 0.2
4-coumaroyl-CoA
0.5
acryloyl-CoA
-
pH and temperature not specified in the publication
0.089 - 0.38
cinnamoyl-CoA
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
0.03
CO2
mutant enzyme T82D, at pH 8.0 and 30°C
0.08
CO2
mutant enzyme S119A, at pH 8.0 and 30°C
0.09
CO2
wild type enzyme, at pH 8.0 and 30°C
0.15
CO2
mutant enzyme F170Y, at pH 8.0 and 30°C
0.155
CO2
mutant enzyme E171A, at pH 8.0 and 30°C
0.2
CO2
-
at pH 7.8, temperature not specified in the publication
0.2
CO2
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
1.31
CO2
mutant enzyme H365N, at pH 8.0 and 30°C
0.01
crotonyl-CoA
mutant enzyme F170Y, at pH 8.0 and 30°C
0.0134
crotonyl-CoA
mutant enzyme T82D, at pH 8.0 and 30°C
0.021
crotonyl-CoA
wild type enzyme, at pH 8.0 and 30°C
0.0298
crotonyl-CoA
mutant enzyme H365N, at pH 8.0 and 30°C
0.031
crotonyl-CoA
mutant enzyme F170A, at pH 8.0 and 30°C
0.036
crotonyl-CoA
mutant enzyme S119A, at pH 8.0 and 30°C
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
0.5
crotonyl-CoA
mutant enzyme E171A, at pH 8.0 and 30°C
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
0.011
NADPH
mutant enzyme F170A, at pH 8.0 and 30°C
0.022
NADPH
mutant enzyme H365N, at pH 8.0 and 30°C
0.03
NADPH
mutant enzyme S119A, at pH 8.0 and 30°C
0.036
NADPH
mutant enzyme F170Y, at pH 8.0 and 30°C
0.037
NADPH
wild type enzyme, at pH 8.0 and 30°C
0.052
NADPH
mutant enzyme T82D, at pH 8.0 and 30°C
0.112
NADPH
mutant enzyme E171A, at pH 8.0 and 30°C
0.7
NADPH
-
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
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104
(2S)-ethylmalonyl-CoA
-
in 100 mM Tris-HCl buffer (pH 7.9), temperature not specified in the publication
0.0735 - 0.109
4-coumaroyl-CoA
0.0688 - 0.0877
cinnamoyl-CoA
0.0675 - 103
crotonyl-CoA
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
0.17
CO2
mutant enzyme T82D, at pH 8.0 and 30°C
1.32
CO2
mutant enzyme S119A, at pH 8.0 and 30°C
5.1
CO2
mutant enzyme E171A, at pH 8.0 and 30°C
7.4
CO2
mutant enzyme H365N, at pH 8.0 and 30°C
56
CO2
mutant enzyme F170Y, at pH 8.0 and 30°C
78
CO2
wild type enzyme, at pH 8.0 and 30°C
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
0.172
crotonyl-CoA
mutant enzyme T82D, at pH 8.0 and 30°C
0.1755
crotonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
1.79
crotonyl-CoA
mutant enzyme S119A, at pH 8.0 and 30°C
5
crotonyl-CoA
mutant enzyme H365N, at pH 8.0 and 30°C
5.1
crotonyl-CoA
mutant enzyme E171A, at pH 8.0 and 30°C
8.3
crotonyl-CoA
mutant enzyme F170A, at pH 8.0 and 30°C
83
crotonyl-CoA
mutant enzyme F170Y, at pH 8.0 and 30°C
103
crotonyl-CoA
wild type enzyme, at pH 8.0 and 30°C
0.157
NADPH
mutant enzyme T82D, at pH 8.0 and 30°C
1.47
NADPH
mutant enzyme S119A, at pH 8.0 and 30°C
6
NADPH
mutant enzyme E171A, at pH 8.0 and 30°C
8.1
NADPH
mutant enzyme H365N, at pH 8.0 and 30°C
11
NADPH
mutant enzyme F170A, at pH 8.0 and 30°C
56
NADPH
mutant enzyme F170Y, at pH 8.0 and 30°C
86
NADPH
wild type enzyme, at pH 8.0 and 30°C
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E171A
the mutant shows reduced activity compared to the wild type enzyme
F170A
in the mutant, the carboxylation activity is decreased to 17% at the expense of increased reduction side reactivity compared to the wild type enzyme
F170Y
the mutant shows a slightly increased substrate inhibition, but otherwise very similar kinetic parameters as the wild type enzyme
H365N
the mutant shows a 20fold decreased activity compared with the wild type enzyme but still displays 93% of carboxylated product, even though the KM for CO2 is raised by more than 1 order of magnitude
N81L
the interaction of the enzyme with CO2 is severely disturbed by the N81L mutation. Stereospecificity of butyryl-CoA formation is almost completely lost in the mutant compared with the wild type enzyme
S119A
the mutant shows almost full carboxylation, but at more than 50fold reduced turnover frequency as compared to the wild type enzyme
T82D
the mutant shows almost full carboxylation, but at more than 50fold reduced turnover frequency as compared to the wild type enzyme
E171A
-
the mutant shows reduced activity compared to the wild type enzyme
-
F170A
-
in the mutant, the carboxylation activity is decreased to 17% at the expense of increased reduction side reactivity compared to the wild type enzyme
-
H365N
-
the mutant shows a 20fold decreased activity compared with the wild type enzyme but still displays 93% of carboxylated product, even though the KM for CO2 is raised by more than 1 order of magnitude
-
N81L
-
the interaction of the enzyme with CO2 is severely disturbed by the N81L mutation. Stereospecificity of butyryl-CoA formation is almost completely lost in the mutant compared with the wild type enzyme
-
S119A
-
the mutant shows almost full carboxylation, but at more than 50fold reduced turnover frequency as compared to the wild type enzyme
-
A182L
the mutant with increased activity selectively catalyzes carboxylation over the regular reduction reaction
V350A
the mutant shows increased activity compared to the wild type enzyme
V350F
the mutant shows increased activity compared to the wild type enzyme
V350G
the mutant shows increased activity compared to the wild type enzyme
A182L
-
the mutant with increased activity selectively catalyzes carboxylation over the regular reduction reaction
-
V350A
-
the mutant shows increased activity compared to the wild type enzyme
-
V350F
-
the mutant shows increased activity compared to the wild type enzyme
-
V350G
-
the mutant shows increased activity compared to the wild type enzyme
-
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Erb, T.J.; Berg, I.A.; Brecht, V.; Mueller, M.; Fuchs, G.; Alber, B.E.
Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway
Proc. Natl. Acad. Sci. USA
104
10631-10636
2007
Methylorubrum extorquens AM1, Streptomyces coelicolor, Cereibacter sphaeroides 2.4.1
brenda
Alber, B.E.
Biotechnological potential of the ethylmalonyl-CoA pathway
Appl. Microbiol. Biotechnol.
89
17-25
2010
Methylorubrum extorquens, Cereibacter sphaeroides, Streptomyces coelicolor
brenda
Erb, T.J.; Brecht, V.; Fuchs, G.; Muller, M.; Alber, B.E.
Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase
Proc. Natl. Acad. Sci. USA
106
8871-8876
2009
Cereibacter sphaeroides
brenda
Yoo, H.G.; Kwon, S.Y.; Kim, S.; Karki, S.; Park, Z.Y.; Kwon, H.J.
Characterization of 2-octenoyl-CoA carboxylase/reductase utilizing pteB from Streptomyce avermitilis
Biosci. Biotechnol. Biochem.
75
1191-1193
2011
Streptomyces avermitilis (Q79ZT3), Streptomyces avermitilis
brenda
Schneider, K.; Asao, M.; Carter, M.S.; Alber, B.E.
Rhodobacter sphaeroides uses a reductive route via propionyl coenzyme A to assimilate 3-hydroxypropionate
J. Bacteriol.
194
225-232
2012
Cereibacter sphaeroides (B8XVS5), Cereibacter sphaeroides
brenda
Hu, B.; Lidstrom, M.
CcrR, a TetR family transcriptional regulator, activates the transcription of a gene of the Ethylmalonyl coenzyme A pathway in Methylobacterium extorquens AM1
J. Bacteriol.
194
2802-2808
2012
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
Zhang, L.; Chen, J.; Mori, T.; Yan, Y.; Liu, W.; Abe, I.
Crystallization and preliminary X-ray diffraction analysis of AntE, a crotonyl-CoA carboxylase/reductase from Streptomyces sp. NRRL 2288
Acta Crystallogr. Sect. F
70
734-737
2014
Streptomyces sp. (M1SQA1), Streptomyces sp. NRRL 2288 (M1SQA1)
brenda
Zhang, L.; Mori, T.; Zheng, Q.; Awakawa, T.; Yan, Y.; Liu, W.; Abe, I.
Rational control of polyketide extender units by structure-based engineering of a crotonyl-CoA carboxylase/reductase in antimycin biosynthesis
Angew. Chem. Int. Ed. Engl.
54
13462-13465
2015
Streptomyces sp. (M1SQA1), Streptomyces sp. NRRL 2288 (M1SQA1)
brenda
Blazic, M.; Kosec, G.; Baebler, S.; Gruden, K.; Petkovic, H.
Roles of the crotonyl-CoA carboxylase/reductase homologues in acetate assimilation and biosynthesis of immunosuppressant FK506 in Streptomyces tsukubaensis
Microb. Cell Fact.
14
164
2015
Streptomyces tsukubensis, Streptomyces tsukubensis NRRL 18488
brenda
Ray, L.; Valentic, T.R.; Miyazawa, T.; Withall, D.M.; Song, L.; Milligan, J.C.; Osada, H.; Takahashi, S.; Tsai, S.C.; Challis, G.L.
A crotonyl-CoA reductase-carboxylase independent pathway for assembly of unusual alkylmalonyl-CoA polyketide synthase extender units
Nat. Commun.
7
13609
2016
Streptomyces ambofaciens, Streptomyces ambofaciens ATCC23877
brenda
Escudero, L.; Al-Refai, M.; Nieto, C.; Laatsch, H.; Malpartida, F.; Seco, E.M.
New rimocidin/CE-108 derivatives obtained by a crotonyl-CoA carboxylase/reductase gene disruption in Streptomyces diastaticus var. 108: substrates for the polyene carboxamide synthase PcsA
PLoS ONE
10
e0135891
2015
Streptomyces diastaticus (Q6T2B7), Streptomyces diastaticus
brenda
Stoffel, G.M.M.; Saez, D.A.; DeMirci, H.; Voegeli, B.; Rao, Y.; Zarzycki, J.; Yoshikuni, Y.; Wakatsuki, S.; Voehringer-Martinez, E.; Erb, T.J.
Four amino acids define the CO2 binding pocket of enoyl-CoA carboxylases/reductases
Proc. Natl. Acad. Sci. USA
116
13964-13969
2019
Kitasatospora setae (E4N096), Kitasatospora setae ATCC 33774 (E4N096)
brenda