Information on EC 1.2.1.80 - long-chain acyl-[acyl-carrier-protein] reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.2.1.80
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RECOMMENDED NAME
GeneOntology No.
long-chain acyl-[acyl-carrier-protein] reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alkane biosynthesis I
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heptadecane biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming)
Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
orf1594 or sll0209
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Manually annotated by BRENDA team
orf1594 or sll0209
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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C-terminal CpFAS1-R enzyme belongs to a multifunctional Type I fatty acid synthase, CpFAS1, with at least 21 enzymatic domains, this megasynthase is predicted to function as a fatty acyl elongase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
fatty acyl-CoA + NAD(P)H + H+
fatty aldehyde + CoA + NAD(P)+
show the reaction diagram
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CpFAS1-R can only utilize very long chain fatty acyl-CoAs as substrates, with activity on C26 > C24 > C22 > C20, but no activity on C18 and C16 or fewer carbons
since aldehydes are toxic to cells it is very likely that the fatty aldehyde is immediately transformed into the corresponding alcohol by the enzyme complex
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?
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
show the reaction diagram
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kinetically preferred and likely the in vivo substrate
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?
fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl-carrier protein + NAD(P)+
show the reaction diagram
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?
hexacosanoyl-CoA + NAD(P)H + H+
hexacosanal + CoA + NAD(P)+
show the reaction diagram
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?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
show the reaction diagram
oleoyl-[acyl carrier protein] + NAD(P)H + H+
oleic aldehyde + acyl carrier protein + NAD(P)+
show the reaction diagram
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?
additional information
?
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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
fatty acyl-[acyl carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl carrier protein + NAD(P)+
show the reaction diagram
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kinetically preferred and likely the in vivo substrate
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?
fatty acyl-[acyl-carrier protein] + NAD(P)H + H+
fatty aldehyde + acyl-carrier protein + NAD(P)+
show the reaction diagram
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-
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?
hexadecanoyl-[acyl-carrier protein] + NAD(P)H + H+
hexadecanal + acyl-carrier protein + NAD(P)+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADPH
additional information
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no significant activity of truncated mAtFAR6 observed when NADH is used as cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.91
hexacosanoyl-CoA
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pH 7.2, temperature not specified in the publication
0.00148
hexadecanoyl-[acyl-carrier protein]
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pH 7.0, at 30°C
0.0079
oleoyl-[acyl carrier protein]
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pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077
hexacosanoyl-CoA
Cryptosporidium parvum
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pH 7.2, temperature not specified in the publication
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
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truncated mAtFAR6 protein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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AtFAR6 promoter active in epidermis, endothecium and tapetum of anthers, histochemical staining of AtFAR6 promoter-GUS reporter gene activity
Manually annotated by BRENDA team
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AtFAR6 promoter active in stem layer, histochemical staining of AtFAR6 promoter-GUS reporter gene activity
Manually annotated by BRENDA team
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AtFAR6 promoter active in the replum and receptacle of siliques
Manually annotated by BRENDA team
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throughout lateral and primary root development, histochemical staining of AtFAR6 promoter-GUS reporter gene activity
Manually annotated by BRENDA team
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histochemical staining of AtFAR6 promoter-GUS reporter gene activity
Manually annotated by BRENDA team
additional information
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no AtFAR6 promoter-GUS reporter gene activity in the inner cortex, vascular bundles or flower microspores
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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transient expression of fusion proteins of AtFAR6 and yellow fluorescent protein in Nicotiana sp. leaves show that AtFAR6 is chloroplast-localized
Manually annotated by BRENDA team
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in Escherichia coli expressed AtFAR6 and mAtFAR6 purified by a HisTrap HP column BioLogic LP liquid chromatography system
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to homogeneity as a maltose-binding protein-fusion protein by amylose-resin based affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AtFAR6 full length version and a truncated version, mAtFAR6, which lacks the chloroplast transit peptide sequence expressed in Escherichia coli, both enzymes fused at the C-terminus to a His Tag containing maltose binding protein; AtFAR6 full length version and a truncated version, mAtFAR6, which lacks the chloroplast transit peptide sequence subcloned into the pYES-DEST52 plasmid downstream of the GAL1 promoter and transformed into Saccharomyces cerevisiae W303-1A strain
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expression of strain PCC7942 orf1593 and orf1594, the latter encoding an aldehde decarbonylase, both separately and together in Escherichia coli. Extracts of recombinant PCC7942_orf1594-expressing cells contain substantial quantities of evenchain fatty aldehydes and fatty alcohols, whereas coexpression of both PCC7942_orf1593 and orf1594 results in the production of odd chain alkanes and alkenes, as well as even-chain fatty aldehydes and fatty alcohols. Orf1593 and orf1594 appear to be part of a larger operon that contains a gene encoding a subunit of the acetyl-CoA carboxylase, accA, which is essential for growth
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in a Rosetta bacterial strain serving as an expression host for the maltose-binding protein-CpFAS1-R fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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since the giant CpFAS1 and polyketide synthase CpPKS1 are structurally and functionally different from human Type I FAS, these parasite megasynthases may serve as novel drug targets, also because CpFAS1 and CpPKS1 utilize R domains to release final products