1.14.19.39: acyl-lipid DELTA12-acetylenase

This is an abbreviated version!
For detailed information about acyl-lipid DELTA12-acetylenase, go to the full flat file.

Reaction

Synonyms

ACET, acetylenase, bifunctional D12/D15 fatty acid desaturase, CREP-1, CREP1, crepenylate synthase linoleate DELTA12-fatty acid acetylenase (desaturase), Crepenynate synthase, Delta-12 fatty acid acetylenase, delta-12 fatty acid desaturase 2, DELTA12 acetylenase, DELTA12 fatty acid desaturase, DELTA12 linoleate acetylenase, DELTA12-desaturase, DELTA12-fatty acid dehydrogenase, DELTA12-fatty acid desaturase, DELTA12-fatty acid desaturases, DELTA12DS, EC 1.14.99.33, FAD2, FAD2-1, FAD2-2, FAT-2, fatty acid DELTA12-desaturase, H6Cf0807, linoleoyl 12-desaturase, microsomal DELTA12-fatty acid desaturase, microsomal omega-6 fatty acid desaturase, oleate desaturase, seed-specific delta-12 fatty acid desaturase 2

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.19 With oxidation of a pair of donors resulting in the reduction of O₂ to two molecules of water

                1.14.19.39 acyl-lipid DELTA12-acetylenase

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Results	in table
1	Activating Compound
74	AA Sequence
1	CAS Registry Number
10	Cloned(Commentary)
7	General Information
1	Inhibitors
13	Localization
1	Metals/Ions
5	Natural Substrates/ Products (Substrates)
13	Organism
2	Pathway
1	Purification (Commentary)
2	Reaction
3	Reaction Type
13	Reference
8	Source Tissue
18	Substrates and Products (Substrate)
2	Subunits
42	Synonyms
1	Systematic Name

Natural Substrates Products

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Natural Substrates Products on EC 1.14.19.39 - acyl-lipid DELTA12-acetylenase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

linoleate + NAD(P)H + O2

crepenynate + NAD(P)+ + H2O

Crepis alpina

-

enzyme is involved in biosynthesis of crepenynic acid

285468

-

285468

?

linoleate + reduced acceptor + O2

crepenynate + acceptor + H2O

Crepis alpina

-

first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters

657528

-

-

?

phosphatidylcholine + reduced cytochrome b5 + O2

? + cytochrome b5 + 2 H2O

Physcomitrium patens

A9RQ27, A9RV06

with NADH

728074

-

-

?

additional information

?

-

3 entries

additional information

?

-

Acanthamoeba castellanii

-

key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview

684454

-

-

?

additional information

?

-

Cantharellus formosus

D9ZGG6

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

-

-

?

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

715539

-

-

?