KEGG   ENZYME: 1.14.19.25
Entry
EC 1.14.19.25               Enzyme                                 

Name
acyl-lipid omega-3 desaturase (cytochrome b5);
FAD3
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
Sysname
(9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (15,16 cis-dehydrogenating)
Reaction(IUBMB)
a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an alpha-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O [RN:R12416]
Reaction(KEGG)
R12416
Substrate
linoleoyl-[glycerolipid] [CPD:C21529];
ferrocytochrome b5 [CPD:C00999];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
alpha-linolenoyl-[glycerolipid] [CPD:C21531];
ferricytochrome b5 [CPD:C00996];
H2O [CPD:C00001]
Comment
This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid. The distance from the carboxylic acid end of the molecule does not have an effect. The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into alpha-linolenoyl groups. The enzyme from the fungus Mortierella alpina acts on gamma-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively [3]. cf. EC 1.14.19.35, sn-2 acyl-lipid omega-3 desaturase (ferredoxin).
History
EC 1.14.19.25 created 2015
Orthology
K10257  acyl-lipid omega-3 desaturase
Genes
AJM: 119045597
CEL: CELE_W02A2.1(fat-2) CELE_Y67H2A.8(fat-1)
CBR: CBG_01790(Cbr-fat-2) CBG_01791(Cbr-fat-1)
BMY: BM_BM6111(Bm6111)
LOA: LOAG_02175
HRO: HELRODRAFT_71572
LGI: LOTGIDRAFT_116269 LOTGIDRAFT_74451
PCAN: 112555112
OBI: 106883679
OSN: 115215637
ATH: AT2G29980(FAD3) AT3G11170(FAD7) AT5G05580(FAD8)
GRA: 105776289(FAD78-2D) 105780050(FAD78-1D) 105786551(FAD78-3D) 105791965(FAD3-2.1D) 105799158(FAD3-1D)
GMX: 100037456(FAD3B) 100217335(FAD8-1) 100305351(FAD7-1) 100499626(FAD7-2) 100799517(FAD8.2) 547470(FAD3C) 547715(FAD3A) 732540(FAD3-2b)
LJA: Lj0g3v0123589.1(Lj0g3v0123589.1) Lj1g3v2337910.1(Lj1g3v2337910.1) Lj2g3v2277520.1(Lj2g3v2277520.1)
CSV: 101209295 101223135(FAD7)
MCHA: 111023722
JCU: 105630235(FAD3) 105646096(FAD) 105646580
SLY: 100134915 544203(Fad7)
NCOL: 116254277
DOSA: Os03t0290300-01(Os03g0290300) Os07t0693800-01(Os07g0693800) Os11t0104400-01(Os11g0104400) Os12t0104400-01(Os12g0104400)
APRO: F751_6504
PTI: PHATRDRAFT_41570(PTD15)
SYN: sll1441(desB)
SYZ: MYO_117450(desB)
SYY: SYNGTS_1727(desB)
SYT: SYNGTI_1727(desB)
SYS: SYNPCCN_1726(desB)
SYQ: SYNPCCP_1726(desB)
SYP: SYNPCC7002_A0159(desB)
AMR: AM1_3759
MAR: MAE_34620(desB)
MPK: VL20_3142
MVZ: myaer102_09850(desB)
CYT: cce_4388
TER: Tery_4492
ANA: all1597
NSH: GXM_01597
AVA: Ava_4210
NAZ: Aazo_3556
CALH: IJ00_05015
DOU: BMF77_00181(desA_2)
CTHE: Chro_2759
LKB: LPTSP3_g23450(desA_1)
 » show all
Reference
1  [PMID:8102138]
  Authors
Browse J, McConn M, James D Jr, Miquel M
  Title
Mutants of Arabidopsis deficient in the synthesis of alpha-linolenate. Biochemical and genetic characterization of the endoplasmic reticulum linoleoyl desaturase.
  Journal
J Biol Chem 268:16345-51 (1993)
  Sequence
[ath:AT2G29980]
Reference
2  [PMID:1455229]
  Authors
Arondel V, Lemieux B, Hwang I, Gibson S, Goodman HM, Somerville CR
  Title
Map-based cloning of a gene controlling omega-3 fatty acid desaturation in Arabidopsis.
  Journal
Science 258:1353-5 (1992)
DOI:10.1126/science.1455229
  Sequence
[brp:103867994]
Reference
3  [PMID:15538555]
  Authors
Sakuradani E, Abe T, Iguchi K, Shimizu S
  Title
A novel fungal omega3-desaturase with wide substrate specificity from arachidonic acid-producing Mortierella alpina 1S-4.
  Journal
Appl Microbiol Biotechnol 66:648-54 (2005)
DOI:10.1007/s00253-004-1760-x
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.25
IUBMB Enzyme Nomenclature: 1.14.19.25
ExPASy - ENZYME nomenclature database: 1.14.19.25
BRENDA, the Enzyme Database: 1.14.19.25

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