Any feedback?
Information on EC 1.3.1.8 - acyl-CoA dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.3.1.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.3.1.8 acyl-CoA dehydrogenase (NADP+)IUBMB Comments
The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].
Specify your search results
Word Map
- 1.3.1.8
- enoyl-coas
- acyl-coas
- crotonyl-coa
-
very-long-chain
-
vlcfas
- butyryl-coa
-
dehydrase
- 3-hydroxyacyl-coa
-
beta-hydroxyacyl-coa
- decanoyl-coa
-
acetyl-coa-dependent
- octanoyl-coa
- elongase
- leek
-
nadph-specific
- collinus
-
trans-enoyl-coas
- synthesis
- biotechnology
The enzyme appears in viruses and cellular organisms
Synonyms
enoyl-coa reductase, 2-enoyl-coa reductase, nbecr, 2-trans-enoyl-coa reductase, crotonyl coa reductase, 2-trans enoyl-coa reductase, enoyl coenzyme a 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
acyl coenzyme A dehydrogenase (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
crotonyl CoA reductase
-
-
-
-
crotonyl coenzyme A reductase
-
-
-
-
crotonyl-CoA reductase
dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
enoyl coenzyme A reductase
-
-
-
-
trans-2-enoyl-CoA reductase
crotonyl-CoA reductase
-
-
-
-
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
acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+
-
-
-
-
acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+
enzyme might also belong to EC 1.3.99.3, acyl-CoA dehydrogenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:NADP+ 2-oxidoreductase
The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37251-07-3
-
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
2-methyl-trans-crotonyl-CoA + NADPH
2-methylbutanoyl-CoA + NADP+
-
2% of trans-crotonyl-CoA activity
-
-
?
2-trans-8,11-eicosatrienoyl-CoA + NADPH
8,11-eicosadienoyl-CoA + NADP+
-
fat-free dietary elevates the activity
-
?
3-butenoyl-CoA + NADPH
butanoyl-CoA + NADP+
-
7% of trans-crotonyl-CoA activity
-
-
?
3-methyl-crotonyl-CoA + NADPH
3-methylbutanoyl-CoA + NADP+
-
17% of trans-crotonyl-CoA activity
-
-
?
5-hydroxyundec-cis-2-enoyl-CoA + NADPH
5-hydroxyundecanoyl-CoA + NADP+
-
-
-
-
?
6,9-octadecadienoyl-CoA + NADPH
?
-
fat-free dietary elevates the activity
-
-
?
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
2-cis-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
-
substrate is not specified as cis- or trans-octenoyl-CoA
-
-
?
2-trans-decenoyl-CoA + NAD(P)H
decanoyl-CoA + NADP+
-
mitochondrial reductase II shows high activity, cofactor NADH
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
15% of trans-crotonyl-CoA activity
-
-
?
2-trans-dodecenoyl-CoA + NAD(P)H
dodecanoyl-CoA + NAD(P)+
-
mitochondrial reductases II and III, low activity, cofactor NADH for isoform II and NADH or NADPH for isoform III
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
13% of trans-crotonyl-CoA activity
-
-
?
2-trans-hexadecenoyl-CoA + NADPH
hexadecanoyl CoA + NADP+
-
-
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
30% of trans-crotonyl-CoA activity
-
-
?
2-trans-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NADP+
-
mitochondrial enzymes, reductase III shows highest activity, reductase I shows 45% activity of that with crotonyl-CoA, reductase II shows lower activity, cofactor NADH for isoform I and II and NADH or NADPH for isoform III
-
-
?
2-trans-octadecenoyl-CoA + NAD(P)H
octadecanoyl-CoA + NAD(P)+
-
cofactor NADH, mitochondrial reductase I shows 25% activity of that with crotonyl-CoA, reductase II shows highest activity
-
-
?
2-trans-octadecenoyl-CoA + NAD(P)H
octadecanoyl-CoA + NAD(P)+
-
i.e. 2-trans-oleoyl-CoA
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
mitochondrial enzyme, NADH-specific reaction
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
substrate is not specified as cis- or trans-octenoyl-CoA
-
-
?
2-trans-octenoyl-CoA + NAD(P)H
octanoyl-CoA + NADP+
-
trans isomer exhibits 1/3 of activity of cis isomer
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
cis-crotonyl-CoA 30% of trans-crotonyl-CoA activity
-
-
?
crotonyl-CoA + NAD(P)H
butanoyl-CoA + NADP+
-
mitochondrial reductase I, no specification of stereoisomer, cofactor NADH
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
enzyme is involved in synthesizing methylmalonyl-CoA precursors for monensin biosynthesis, pathway flux, overview
-
-
?
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
-
r
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme activity is higher in neurological Trembler mouse mutant than in wild-type
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
-
i.e. arachidoyl-CoA
?
additional information
?
-
-
no cis-isomeric substrates tested, classification is not definite
-
-
?
additional information
?
-
-
no activity with acetoacetyl-CoA or (R)-3-hydroxybutyryl-CoA
-
-
?
additional information
?
-
-
mitochondrial reductase III uses substrate with chain length of C4-C12
-
-
?
additional information
?
-
-
no cis-isomeric substrates tested, classification is not definite
-
-
?
additional information
?
-
-
active as part of fatty acid synthetase by incorporation of acetyl-CoA in mitochondria and of malonyl-CoA in cytosol
-
-
?
additional information
?
-
-
very slow reduction of substrate with chain length C4, C10, C12
-
-
?
additional information
?
-
-
FMN is essential for the reaction, tightly bound to apoprotein
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
?
additional information
?
-
-
specific for alpha/beta-unsaturated CoA derivatives with chain lengths of 4-16 C atoms, neither involved in beta-oxidation of fatty acids nor de novo-synthesis of fatty acids via malonyl-CoA
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
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
5-hydroxyundec-cis-2-enoyl-CoA + NADPH
5-hydroxyundecanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
enzyme is involved in synthesizing methylmalonyl-CoA precursors for monensin biosynthesis, pathway flux, overview
-
-
?
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme is part of acyl-CoA elongase complex responsible for fatty acid elongation
-
?
trans-2-eicosenoyl-CoA + NADPH
eicosanoyl-CoA + NADP+
-
enzyme activity is higher in neurological Trembler mouse mutant than in wild-type
-
?
additional information
?
-
-
active as part of fatty acid synthetase by incorporation of acetyl-CoA in mitochondria and of malonyl-CoA in cytosol
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
the enzyme catalyzes the last step in synthesis of very long fatty acid. NbECR activity is essential for membrane biogenesis. Loss of NbECR function affects biogenesis of cellular membranes including the plasma membrane and the thylakoid membrane
-
-
?
additional information
?
-
-
specific for alpha/beta-unsaturated CoA derivatives with chain lengths of 4-16 C atoms, neither involved in beta-oxidation of fatty acids nor de novo-synthesis of fatty acids via malonyl-CoA
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
additional information
?
-
-
involvement in malonyl-CoA fatty acid elongation system II
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
1 mol per mol of protein, prosthetic group is essentiell for the reaction
NADH
-
20fold higher concentration of NADH compared to NADPH results in 50% of NADPH activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-trans-octadecenoyl-CoA
-
without bovine serum albumin substrate-induced inhibition at 0.02-0.03 mM
palmitoyl-CoA
-
without bovine serum albumin substrate-induced inhibition at 0.02-0.03 mM
pyridoxal 5'-phosphate
-
competitive with NADPH, 80% inactivation at 1 mM, reversibel
trans-2-hexenoyl-CoA
-
competitive inhibition of crotonoyl-CoA reduction, but not of 2-trans-hexadecenoyl-CoA and 2-trans-decenoyl-CoA reduction
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
additional information
-
bovine serum albumin in assay mixture elevated the activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Arginyl residues are involved in acyl-CoA binding to the elongase from etiolated leek seedlings.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1