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Information on EC 1.3.1.85 - crotonyl-CoA carboxylase/reductase and Organism(s) Cereibacter sphaeroides and UniProt Accession Q3IZ91

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IUBMB 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).
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Cereibacter sphaeroides
UNIPROT: Q3IZ91
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The taxonomic range for the selected organisms is: Cereibacter sphaeroides
The enzyme appears in selected viruses and cellular organisms
Synonyms
crotonyl-coa carboxylase/reductase, 2-octenoyl-coa carboxylase/reductase, enoyl-coa carboxylase/reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
crotonyl-CoA reductase (carboxylating)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
show the reaction diagram
-
100% relative specific activity, the carboxylation reaction is the physiologically relevant reaction
-
-
r
(E)-crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
show the reaction diagram
-
10% of maximal activity (compared with vmax of crotonyl-CoA carboxylation)
-
-
?
acryloyl-CoA + CO2 + NADPH + H+
methylmalonyl-CoA + NADP+
show the reaction diagram
-
acryloyl-CoA is accepted as an alternative substrate analogue by the enzyme with 40% relative activity (compared with vmax of crotonyl-CoA carboxylation)
-
-
?
crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(E)-crotonyl-CoA + CO2 + NADPH + H+
(2S)-ethylmalonyl-CoA + NADP+
show the reaction diagram
-
100% relative specific activity, the carboxylation reaction is the physiologically relevant reaction
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
B8XVS5
activity is upregulated during photoheterotrophic growth on acetate compared to the activities during growth on succinate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.4
(E)-crotonyl-CoA
0.5
acryloyl-CoA
-
pH and temperature not specified in the publication
0.2
CO2
-
at pH 7.8, temperature not specified in the publication
0.7
NADPH
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
B8XVS5
crotonyl-CoA carboxylase/reductase, a key enzyme of the ethylmalonyl-CoA pathway for acetyl-CoA assimilation, is not essential for growth with 3-hydroxypropionate
metabolism
-
the unique reductive carboxylation of crotonyl-CoA by the enzyme crotonyl-CoA carboxylase/reductase can be considered the committed step for acetyl-CoA assimilation by the ethylmalonyl-CoA pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
gel filtration
47000
-
2 * 47000, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 47000, gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
although the reaction is reversible, the activity of crotonyl-CoA carboxylase/reductase is up-regulated at least 60fold for Rhodobacter sphaeroides during growth with acetate versus succinate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alber, B.E.
Biotechnological potential of the ethylmalonyl-CoA pathway
Appl. Microbiol. Biotechnol.
89
17-25
2010
Cereibacter sphaeroides, Methylorubrum extorquens, Streptomyces coelicolor
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team