Enzyme

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     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
ID:1.14.19.45
Description:sn-1 oleoyl-lipid 12-desaturase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.19.45
BRENDA Enzyme Link: BRENDA 1.14.19.45
KEGG Enzyme Link: KEGG1.14.19.45
BioCyc Enzyme Link: BioCyc 1.14.19.45
ExPASy Enzyme Link: ExPASy1.14.19.45
EC2PDB Enzyme Link: EC2PDB 1.14.19.45
ExplorEnz Enzyme Link: ExplorEnz 1.14.19.45
PRIAM enzyme-specific profiles Link: PRIAM 1.14.19.45
IntEnz Enzyme Link: IntEnz 1.14.19.45
MEDLINE Enzyme Link: MEDLINE 1.14.19.45
MSA:

1.14.19.45;

Phylogenetic Tree:

1.14.19.45;

Uniprot:
M-CSA:
RHEA:46776 a 1-[(9Z)-octadecenoyl]-2-acyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-[(9Z,12Z)-octadecdienoyl]-2-acyl-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[Fe;H0;+0:6]-[*:7].[*:8]-[Fe;H0;+0:9]-[*:10].[H+;H0:11].[H+;H0:12].[O;H0;+0:13]=[O;H0;+0:14]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]-[Fe+;H0:6]-[*:7].[*:8]-[Fe+;H0:9]-[*:10].[OH2;+0:13].[OH2;+0:14]
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References

TitleAuthorsDatePubMed ID
Expression of acyl-lipid Delta12-desaturase gene in prokaryotic and eukaryotic cells and its effect on cold stress tolerance of potato.Amiri RM, Yur'eva NO, Shimshilashvili KR, Goldenkova-Pavlova IV, Pchelkin VP, Kuznitsova EI, Tsydendambaev VD, Trunova TI, Los DA, Jouzani GS, Nosov AM2010 Mar20377689
An in Vivo Study of Substrate Specificities of Acyl-Lipid Desaturases and Acyltransferases in Lipid Synthesis in Synechocystis PCC6803.Higashi S, Murata N1993 Aug12231903
Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation.Wada H, Gombos Z, Murata N1990 Sep 132118597