| EC |
1.14.19.28 |
| Accepted name: |
sn-1 stearoyl-lipid 9-desaturase |
| Reaction: |
a 1-stearoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-oleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O |
| Other name(s): |
desC (gene name) |
| Systematic name: |
1-stearoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating) |
| Comments: |
The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 9 of stearoyl groups (18:0) attached to the sn-1 position of glycerolipids. The enzyme is nonspecific with respect to the polar head group of the glycerolipid. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Wada, H., Schmidt, H., Heinz, E. and Murata, N. In vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. J. Bacteriol. 175 (1993) 544–547. [DOI] [PMID: 8419301] |
| 2. |
Higashi, S. and Murata, N. An in vivo study of substrate specificities of acyl-lipid desaturases and acyltransferases in lipid synthesis in Synechocystis PCC6803. Plant Physiol. 102 (1993) 1275–1278. [PMID: 12231903] |
| 3. |
Sakamoto, T., Wada, H., Nishida, I., Ohmori, M. and Murata, N. Δ9 Acyl-lipid desaturases of cyanobacteria. Molecular cloning and substrate specificities in terms of fatty acids, sn-positions, and polar head groups. J. Biol. Chem. 269 (1994) 25576–25580. [PMID: 7929259] |
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| [EC 1.14.19.28 created 2015] |
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