BRENDA - Enzyme Database show
show all sequences of 1.14.19.39

Functional diversity in fungal fatty acid synthesis: the first acetylenase from the Pacific golden chanterelle, Cantharellus formosus

Blacklock, B.J.; Scheffler, B.E.; Shepard, M.R.; Jayasuriya, N.; Minto, R.E.; J. Biol. Chem. 285, 28442-28449 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene Cf0807 or CfACET, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged ACTE in Saccharomyces cerevisiae
Cantharellus formosus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
the enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
Cantharellus formosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Cantharellus formosus
H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cantharellus formosus
D9ZGG6
gene Cf0807 or CfACET
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
fruit body
-
Cantharellus formosus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
715539
Cantharellus formosus
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Cf0807 or CfACET, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged ACTE in Saccharomyces cerevisiae
Cantharellus formosus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
the enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
Cantharellus formosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Cantharellus formosus
H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
fruit body
-
Cantharellus formosus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
H6Cf0807 is an acetylenase, that produces a trans DELTA12 double bond, while H6Cf0745 is a classical FAD2 desaturase. The Cantharellus formosus FAD2 homologue H6Cf0745 expression results in the production of only 16:2 DELTA9,12 and 18:2 DELTA9,12 in recombinant yeast cells supplemented with 18:2 DELTA9c,12c. Expression ofH6Cf0807 results in the production of crepenynic acid, 18:1 DELTA9c,12a. No C16 acetylenic fatty acid is detected. Supplementation with 18:2 DELTA9c,12t, alpha-linolenic acid, 18:3 DELTA9,12,15, or gamma-linolenic acid, 18:3 DELTA6,9,12, does not result in the production of other fatty acids, overview
715539
Cantharellus formosus
?
-
-
-
-
General Information
General Information
Commentary
Organism
metabolism
the bifunctional desaturase and the acetylenase provide the enzymatic activities required to drive oleate through linoleate to crepenynate and the conjugated enyne (14Z)-dehydrocrepenynate, the branchpoint precursors to a major class of acetylenic natural products, biosynthesis of polyacetylenic metabolites in Basidiomycetes, overview
Cantharellus formosus
additional information
the acetylenase gene, identified from the fungus, is phylogenetically distinct from known plant and fungal desaturases. The enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
Cantharellus formosus
physiological function
to produce the accumulated natural product dehydrocrepenynic acid, chanterelle must have both FAD2/3 desaturase, EC 1.14.19.6. and acetylenase activities, production of the trans DELTA12 double bond by H6Cf0807
Cantharellus formosus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the bifunctional desaturase and the acetylenase provide the enzymatic activities required to drive oleate through linoleate to crepenynate and the conjugated enyne (14Z)-dehydrocrepenynate, the branchpoint precursors to a major class of acetylenic natural products, biosynthesis of polyacetylenic metabolites in Basidiomycetes, overview
Cantharellus formosus
additional information
the acetylenase gene, identified from the fungus, is phylogenetically distinct from known plant and fungal desaturases. The enzyme contains positionally conserved histidine box motifs that are believed to bind two active-site iron atoms and are critical to enzyme function
Cantharellus formosus
physiological function
to produce the accumulated natural product dehydrocrepenynic acid, chanterelle must have both FAD2/3 desaturase, EC 1.14.19.6. and acetylenase activities, production of the trans DELTA12 double bond by H6Cf0807
Cantharellus formosus
Other publictions for EC 1.14.19.39
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745739
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41
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715539
Blacklock
Functional diversity in fungal ...
Cantharellus formosus
J. Biol. Chem.
285
28442-28449
2010
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Cloning and transcriptional an ...
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52-57
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Properties of two multifunctio ...
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Synthesis and conformational s ...
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285468
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