The Enzyme Database

Your query returned 2 entries.    printer_iconPrintable version

EC 1.14.19.33     
Accepted name: Δ12 acyl-lipid conjugase (11E,13E-forming)
Reaction: (1) a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an α-eleostearoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) a γ-linolenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an α-parinaroyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: α-eleostearate = (9Z,11E,13E)-octadeca-9,11,13-trienoate
α-parinarate = (9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate
γ-linolenic acid = (6Z,9Z,12Z)-octadeca-6,9,12-trienoic acid
linoleic acid = (9Z,12Z)-octadeca-9,12-dienoic acid
Other name(s): fatty acid Δ12-conjugase (ambiguous); FADX (gene name)
Systematic name: Δ12 acyl-lipid,ferrocytochrome-b5:oxygen 11,14 allylic oxidase (11E,13E-forming)
Comments: The enzyme, characterized from the plants Impatiens balsamina, Momordica charantia (bitter gourd) and Vernicia fordii (tung tree), converts a single cis double bond at carbon 12 to two conjugated trans bonds at positions 11 and 13. The enzyme from Vernicia fordii can also act as a 12(E) desaturase when acting on the monounsaturated fatty acids oleate and palmitoleate. cf. EC 1.14.19.16, linoleoyl-lipid Δ12 conjugase (11E,13Z-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cahoon, E.B., Carlson, T.J., Ripp, K.G., Schweiger, B.J., Cook, G.A., Hall, S.E. and Kinney, A.J. Biosynthetic origin of conjugated double bonds: production of fatty acid components of high-value drying oils in transgenic soybean embryos. Proc. Natl. Acad. Sci. USA 96 (1999) 12935–12940. [DOI] [PMID: 10536026]
2.  Dyer, J.M., Chapital, D.C., Kuan, J.C., Mullen, R.T., Turner, C., McKeon, T.A. and Pepperman, A.B. Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity. Plant Physiol. 130 (2002) 2027–2038. [DOI] [PMID: 12481086]
[EC 1.14.19.33 created 2015]
 
 
EC 1.14.19.46     
Accepted name: sn-1 linoleoyl-lipid 6-desaturase
Reaction: a 1-linoleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-γ-linolenoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): desD (gene name)
Systematic name: 1-linoleoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (6,7-cis-dehydrogenating)
Comments: The enzyme, characterized from cyanobacteria, introduces a cis double bond at carbon 6 of linoleoyl groups (18:2) attached to the sn-1 position of glycerolipids. The enzyme is a front-end desaturase, introducing the new double bond between a pre-existing double bond and the carboxyl-end of the fatty acid. It is nonspecific with respect to the polar head group of the glycerolipid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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]
2.  Reddy, A.S. and Thomas, T.L. Expression of a cyanobacterial Δ6-desaturase gene results in γ-linolenic acid production in transgenic plants. Nat. Biotechnol. 14 (1996) 639–642. [DOI] [PMID: 9630958]
3.  Kurdrid, P., Subudhi, S., Hongsthong, A., Ruengjitchatchawalya, M. and Tanticharoen, M. Functional expression of Spirulina6 desaturase gene in yeast, Saccharomyces cerevisiae. Mol. Biol. Rep. 32 (2005) 215–226. [DOI] [PMID: 16328883]
[EC 1.14.19.46 created 2015]
 
 


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