The Enzyme Database

Your query returned 2 entries.    printer_iconPrintable version

EC 1.14.19.36     
Accepted name: sn-1 acyl-lipid ω-3 desaturase (ferredoxin)
Reaction: (1) a 1-γ-linolenoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-stearidonoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(2) a 1-linoleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-α-linolenoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Glossary: stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid
Other name(s): desB (gene name)
Systematic name: 1-γ-linolenoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (15,16 cis-dehydrogenating)
Comments: The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 15 of linoleoyl and γ-linolenoyl groups attached to the sn-1 position of glycerolipids. The enzyme is an ω desaturase, and determines the location of the double bond by counting three carbons from the methyl end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sakamoto, T., Los, D.A., Higashi, S., Wada, H., Nishida, I., Ohmori, M. and Murata, N. Cloning of ω3 desaturase from cyanobacteria and its use in altering the degree of membrane-lipid unsaturation. Plant Mol. Biol. 26 (1994) 249–263. [PMID: 7524725]
[EC 1.14.19.36 created 2015]
 
 
EC 1.14.19.47     
Accepted name: acyl-lipid (9-3)-desaturase
Reaction: (1) an α-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a stearidonoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a γ-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: stearidonic acid = (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid
Other name(s): DES6 (gene name); acyl-lipid 6-desaturase; acyl-lipid Δ6-desaturase; Δ6-desaturase (ambiguous)
Systematic name: Δ9 acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (6,7-cis-dehydrogenating)
Comments: The enzyme, characterized from the moss Physcomitrella patens and the plant Borago officinalis (borage), introduces a cis double bond at carbon 6 of several acyl-lipids that contain an existing Δ9 cis double bond. The enzyme contains a cytochrome b5 domain that acts as the electron donor for the active site of the desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sayanova, O., Smith, M.A., Lapinskas, P., Stobart, A.K., Dobson, G., Christie, W.W., Shewry, P.R. and Napier, J.A. Expression of a borage desaturase cDNA containing an N-terminal cytochrome b5 domain results in the accumulation of high levels of Δ6-desaturated fatty acids in transgenic tobacco. Proc. Natl. Acad. Sci. USA 94 (1997) 4211–4216. [DOI] [PMID: 9108131]
2.  Girke, T., Schmidt, H., Zähringer, U., Reski, R. and Heinz, E. Identification of a novel Δ6-acyl-group desaturase by targeted gene disruption in Physcomitrella patens. Plant J. 15 (1998) 39–48. [DOI] [PMID: 9744093]
[EC 1.14.19.47 created 2015]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald