Information on EC 1.14.19.26 - acyl-[acyl-carrier-protein] 6-desaturase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.19.26
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RECOMMENDED NAME
GeneOntology No.
acyl-[acyl-carrier-protein] 6-desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = (6Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sapienate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
palmitoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (6,7 cis-dehydrogenating)
The enzyme, characterized from the endosperm of the plant Thunbergia alata (black-eyed Susan vine), introduces a cis double bond at carbon 6 of several saturated acyl-[acp]s. It is most active with palmitoyl-[acp] (16:0), but can also act on myristoyl-[acp] (14:0) and stearoyl-[acp] (18:0). The position of the double bond is determined by its distance from the carboxyl end of the fatty acid.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + ferrocytochrome b5 + O2 + H+
stearidonic acid + ferricytochrome b5 + H2O
show the reaction diagram
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?
myristoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster+ O2 + 2 H+
(Z)-tetradec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
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?
oleic acid + ferrocytochrome b5 + O2 + H+
?
show the reaction diagram
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?
palmitoleic acid + ferrocytochrome b5 + O2 + H+
?
show the reaction diagram
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?
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
(Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
(Z)-octadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
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?
additional information
?
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the fatty acids 16:3DELTA7,10,13, 20:2DELTA8,11, 20:3DELTA8,11,14 and 20:4DELTA5,8,11,14 do not serve as substrates
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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
alpha-linolenic acid + ferrocytochrome b5 + O2 + H+
stearidonic acid + ferricytochrome b5 + H2O
show the reaction diagram
A7UFH0
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?
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
(Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b5
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Ferredoxin
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
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loss of most of the desaturase activity
KCN
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1 mM, loss of most of the desaturase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
palmitoyl-[acyl-carrier protein]
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Km-values determined for the wild-type enzyme and mutant A188G/Y189F are in the range of 0.2 to 0.6 mM with both 16:0- and 18:0-[acyl-carrier protein], suggesting that, at least in the case of these enzymes, changes in the substrate binding properties can be discounted as an underlying cause of differences in activities
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain InvSc1
expression in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dexamethasone at a dose of 1 mg/rat produces a significant decrease in microsomal DELTA6 desaturation activity 12 h after the injection
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A181T/A188G/Y189F/S205N/L206T/G207A
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the mutation yields an enzyme that functions primarily as a DELTA9-18:0-[acyl-carrier protein] desaturase. This enzyme displays only DELTA9 desaturase activity with 18:0-[acyl-carrier protein] and is nearly 4-fold more active with this substrate than with 16:0-[acyl-carrier protein]. Like mutant A181TyA200F, this enzyme retains DELTA6 desaturase activity with 16:0-[acyl-carrier protein]
A181T/A200F
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the mutation gives rise to an enzyme that catalyzed primarily the DELTA9 desaturation of 18:0-[acyl-carrier protein], but functions as a DELTA6 desaturase with 16:0-[acyl-carrier protein]
A181T/A200F/S205N/L206T/G207A
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replacement of specific amino acid residues in a DELTA6-palmitoyl (16:0)-[acyl-carrier protein] desaturase with their equivalents from a DELTA9-stearoyl (18:0)-[acyl-carrier protein] desaturase. The A181T/A200F/S205N/L206T/G207A mutant enzyme is functions principally as a DELTA9-18:0-[acyl-carrier protein] desaturase
A188G/Y189F
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mutant with broadened fatty acid chain-length specificity
additional information
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replacement of specific amino acid residues in a DELTA6-palmitoyl (16:0)-[acyl-carrier protein] desaturase with their equivalents from a DELTA9-stearoyl (18:0)-[acyl-carrier protein] desaturase, mutant enzymes are identified that have altered fatty acid chain-length specificities or that can insert double bonds into either the DELTA6 or DELTA9 positions of 16:0- and 18:0-[acyl-carrier protein]
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.19.26)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)