Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.1.10 - enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38071

for references in articles please use BRENDA:EC1.3.1.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38071
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
enoyl reductase, enoyl-acp reductase, enoyl-acyl carrier protein reductase, etr1p, fabl2, mrf1p, enoyl-[acyl-carrier-protein] reductase, enoyl acyl-carrier-protein reductase, 2-enoyl thioester reductase, 2-trans-enoyl-acp reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-enoyl thioester reductase
-
enoyl thioester reductase
-
2-trans-enoyl-ACP reductase
-
-
acyl-ACP dehydrogenase
-
-
-
-
enoyl acyl-carrier-protein reductase
-
-
-
-
enoyl-ACP reductase
-
-
-
-
NADPH 2-enoyl Co A reductase
-
-
-
-
reductase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
additional information
enzyme belongs to the medium-chain dehydrogenase/reductase superfamily of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
anti addition via 2Si,3Si attack on double bond
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Si-specific)
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase system, an enzyme found in yeasts (Ascomycota and Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).
CAS REGISTRY NUMBER
COMMENTARY hide
37251-09-5
-
37251-09-5
not distinguished from EC 1.3.1.39
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
2-trans-hexenoyl-CoA + NADPH
?
show the reaction diagram
-
assay at pH 7.5, 23°C
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
show the reaction diagram
-
stereochemistry
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
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
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
show the reaction diagram
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
specific for form B, i.e. hydrogen in position HB is transferred to substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme Mrf1p
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y73N
site-directed mutagenesis, mutant shows native fold, but only residual wild-type enzyme activity, no rescue of the enzyme-deficient mutant strain mrf1DELTA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme and mutant Y73N from mutant strain BJ1991 mrf1DELTA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of wild-type enzyme and mutant Y73N in enzyme-deficient mutant strain BJ1991 mrf1DELTA, using the catalase 1 promotor
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription factor Adr1p influences transcription levels of ETR1 promoter, which controls the expression of 2-trans-enoyl-ACP reductase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sedgwick, B.; Morris, C.
Stereochemical course of hydrogen transfer catalysed be the enoyl reductase enzyme of the yeast fatty acid synthethase
J. Chem. Soc. Chem. Commun.
1980
96-97
1980
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Seyama, Y.; Kasama, T.; Yamakawa, T.; Kawaguchi, A.; Saito, K.; Okuda, S.
Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase
J. Biochem.
82
1325-1329
1977
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Airenne, T.T.; Torkko, J.M.; Van den plas, S.; Sormunen, R.T.; Kastaniotis, A.J.; Wierenga, R.K.; Kalervo Hiltunen, J.
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance
J. Mol. Biol.
327
47-59
2003
Candida tropicalis, Saccharomyces cerevisiae (P38071), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gurvitz, A.
A novel circuit overrides Adr1p control during expression of Saccharomyces cerevisiae 2-trans-enoyl-ACP reductase Etr1p of mitochondrial type 2 fatty acid synthase
FEMS Microbiol. Lett.
297
255-260
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team