KEGG   ENZYME: 1.14.19.28
Entry
EC 1.14.19.28               Enzyme                                 

Name
sn-1 stearoyl-lipid 9-desaturase;
desC (gene name)
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
1-stearoyl-2-acyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating)
Reaction(IUBMB)
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
Substrate
1-stearoyl-2-acyl-[glycerolipid];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
O2 [CPD:C00007];
H+ [CPD:C00080]
Product
1-oleoyl-2-acyl-[glycerolipid];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]
Comment
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.
History
EC 1.14.19.28 created 2015
Orthology
K23054  sn-1 stearoyl-lipid 9-desaturase
Genes
LAB: LA76x_3785
LAQ: GLA29479_942
LCP: LC55x_3788
LGU: LG3211_1428
PFV: Psefu_1593
HJA: BST95_06850
MNR: ACZ75_23535
BEBA: BWI17_00040 BWI17_10345
CCX: COCOR_04747
MFU: LILAB_00410
SCL: sce0690
MDI: METDI0702
MCH: Mchl_0732
MPO: Mpop_2228
MALU: KU6B_40580(desC3)
BEX: A11Q_2549
NFA: NFA_22050
AMN: RAM_28475
AMM: AMES_5512
AMZ: B737_5512
SYN: sll0541(desC(des9))
SYZ: MYO_125630(desC(des9))
SYY: SYNGTS_2538(desC)
SYT: SYNGTI_2537(desC)
SYS: SYNPCCN_2536(desC)
SYQ: SYNPCCP_2536(desC)
SYJ: D082_16540(desC)
SYC: syc1549_d(desC)
SYW: SYNW2377(desC)
SYX: SynWH7803_2415(desC) SynWH7803_2417(desC)
SYP: SYNPCC7002_A2198(desC)
SYNR: KR49_08200
SYND: KR52_03225
SYH: Syncc8109_2618(desC)
TEL: tlr1653(desC2) tlr2380(desC1)
THN: NK55_04900(desC2) NK55_11555(desC)
TVN: NIES2134_107740(desC1) NIES2134_115680(desC2)
PMA: Pro_1833(OLE1)
PMM: PMM1672(des9)
PMB: A9601_18811(ole1)
PMC: P9515_18621(ole1)
PMG: P9301_18621(ole1)
PMH: P9215_19451(ole1)
PMJ: P9211_17991(ole1)
PME: NATL1_21421(ole1)
PRC: EW14_2040
PRM: EW15_2227
AMR: AM1_1527
CHON: NIES4102_12720(desC)
MAR: MAE_50330(desC)
MPK: VL20_2979
MVZ: myaer102_23510(desC)
CYL: AA637_05810(desC)
CYT: cce_3100(desC1)
TER: Tery_1437
ARP: NIES39_L02040(desC)
PAGH: NIES204_34440(desC)
GVI: gvip170(desC)
GLJ: GKIL_3522(desC)
ANA: all1599(desC)
NSH: GXM_01593
AVA: Ava_4212
NAZ: Aazo_3554
CALH: IJ00_05005
CTHE: Chro_4139
STAN: STA3757_26310(desC)
CEO: ETSB_1681(desC)
CER: RGRSB_1326(desC)
SACI: Sinac_3004
FLN: FLA_5482
MUC: MuYL_3330
HSW: Hsw_2919
 » show all
Reference
1  [PMID:8419301]
  Authors
Wada H, Schmidt H, Heinz E, Murata N
  Title
In vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes.
  Journal
J Bacteriol 175:544-7 (1993)
DOI:10.1128/JB.175.2.544-547.1993
Reference
2  [PMID:12231903]
  Authors
Higashi S, Murata N
  Title
An in Vivo Study of Substrate Specificities of Acyl-Lipid Desaturases and Acyltransferases in Lipid Synthesis in Synechocystis PCC6803.
  Journal
Plant Physiol 102:1275-1278 (1993)
DOI:10.1104/pp.102.4.1275
Reference
3  [PMID:7929259]
  Authors
Sakamoto T, Wada H, Nishida I, Ohmori M, Murata N
  Title
delta 9 Acyl-lipid desaturases of cyanobacteria. Molecular cloning and substrate  specificities in terms of fatty acids, sn-positions, and polar head groups.
  Journal
J Biol Chem 269:25576-80 (1994)
  Sequence
[syn:sll0541] [ana:all1599]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.28
IUBMB Enzyme Nomenclature: 1.14.19.28
ExPASy - ENZYME nomenclature database: 1.14.19.28
BRENDA, the Enzyme Database: 1.14.19.28

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