Information on EC 1.3.8.5 - 2-methyl-branched-chain-enoyl-CoA reductase

Word Map on EC 1.3.8.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Ascaris suum

EC NUMBER
COMMENTARY hide
1.3.8.5
-
RECOMMENDED NAME
GeneOntology No.
2-methyl-branched-chain-enoyl-CoA reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-methylbutanoate biosynthesis
-
-
L-isoleucine degradation I
-
-
SYSTEMATIC NAME
IUBMB Comments
2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase
A flavoprotein (FAD) from Ascaris suum. The enzyme functions in shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA
CAS REGISTRY NUMBER
COMMENTARY hide
122320-06-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methylbutanoyl-CoA + electron-transfer flavoprotein
(E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
show the reaction diagram
-
-
-
2-methylpentanoyl-CoA + electron-transfer flavoprotein
2-methyl-2-pentenoyl-CoA + reduced electron-transfer flavoprotein + H+
show the reaction diagram
98% of the activity with 2-methylbutanoyl-CoA
-
-
butyryl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
show the reaction diagram
13.6% of the activity with 2-methylbutanoyl-CoA
-
-
-
octanoyl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
show the reaction diagram
12.8% of the activity with 2-methylbutanoyl-CoA
-
-
-
pentanoyl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
show the reaction diagram
14.4% of the activity with 2-methylbutanoyl-CoA
-
-
-
additional information
?
-
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
contains 0.9 mol of FAD per mol of subunit
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-2-methyl-2-butenoyl-CoA
-
acetoacetyl-CoA
-
crotonyl-CoA
-
decanoyl-CoA
-
Hexanoyl-CoA
-
NEM
little effect
p-hydroxymercuribenzoate
little effect
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
2-methylbutanoyl-CoA
-
0.021
2-Methylpentanoyl-CoA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.58
2-methylpentanoyl-CoA
1.62
2-methylbutanoyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
2 isoforms of the enzyme: ECRI and ECRII
Manually annotated by BRENDA team
additional information
-
not detected in: early, aerobic larval stages or adult testis, ovary, or intstine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer, pH 7.4, 10% glycerol, stable for at least 30 days
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme form ECRI; the enzyme forms ECRI and ECRII appear to be encoded by separate genes
-
full-length cDNA clones of both reductase isoforms isolated, cloned, and sequenced
-
full-length cDNA coding for the major isoform of the enzyme, ECRI, cloned and sequenced and compared with that of the minor isoform of the enzyme, ECRII
-