KEGG   ENZYME: 1.14.19.44Help
Entry
EC 1.14.19.44               Enzyme                                 

Name
acyl-CoA (8-3)-desaturase;
FADS1 (gene name);
acyl-CoA 5-desaturase (methylene-interrupted)
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
BRITE hierarchy
Sysname
Delta8-acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (5,6-cis-dehydrogenating)
Reaction(IUBMB)
(1) (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = arachidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O [RN:R11059];
(2) (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-CoA + 2 ferricytochrome b5 + 2 H2O [RN:R11060]
Reaction(KEGG)
R11059 R11060;
(other) R12169
Show
Substrate
(8Z,11Z,14Z)-icosa-8,11,14-trienoyl-CoA [CPD:C03595];
ferrocytochrome b5 [CPD:C00999];
O2 [CPD:C00007];
H+ [CPD:C00080];
(8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-CoA [CPD:C16164]
Product
arachidonoyl-CoA [CPD:C02249];
ferricytochrome b5 [CPD:C00996];
H2O [CPD:C00001];
(5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-CoA [CPD:C16165]
Comment
The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8. The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyse the desaturation of dihomo-gamma-linoleate [(8Z,11Z,14Z)-icosa-8,11,14-trienoate] and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37, acyl-CoA 5-desaturase.
History
EC 1.14.19.44 created 2015
Pathway
ec01040  Biosynthesis of unsaturated fatty acids
Orthology
K10224  acyl-CoA (8-3)-desaturase (Delta-5 desaturase)
Genes
HSA: 3992(FADS1)
PTR: 451243(FADS1)
PPS: 100981162(FADS1)
GGO: 101136185(FADS1)
PON: 100436159(FADS1)
NLE: 100596120(FADS1)
MCC: 722343(FADS1)
MCF: 101864778(FADS1)
CSAB: 103234224(FADS1)
RRO: 104679375(FADS1)
RBB: 108533599(FADS1)
CJC: 100389579(FADS1)
SBQ: 101052172(FADS1)
MMU: 76267(Fads1)
MCAL: 110285897(Fads1)
MPAH: 110322451(Fads1)
RNO: 84575(Fads1)
MUN: 110548091(Fads1)
CGE: 100773095
NGI: 103729124(Fads1)
HGL: 101698014(Fads1)
CCAN: 109685566(Fads1)
OCU: 100342403(FADS1)
TUP: 102500595(FADS1)
CFA: 483793
VVP: 112911088(FADS1)
AML: 100472955(FADS1)
UMR: 103678230(FADS1)
UAH: 113246984(FADS1)
ORO: 101364825(FADS1)
FCA: 101083966(FADS1)
PTG: 102968608(FADS1)
AJU: 106986968(FADS1)
BTA: 533107(FADS1)
BOM: 102276098(FADS1)
BIU: 109554369(FADS1)
BBUB: 102405648(FADS1)
PHD: 102315978(FADS1)
CHX: 102178247(FADS1)
OAS: 101109049(FADS1)
SSC: 444995(FADS1)
CFR: 102506763(FADS1)
CDK: 105094872(FADS1)
BACU: 103008410(FADS1)
LVE: 103082696(FADS1)
OOR: 101275971(FADS1)
DLE: 111183884(FADS1)
ECB: 102150261(FADS1)
EPZ: 103543089(FADS1)
EAI: 106847567(FADS1)
MYB: 102261592(FADS1)
MYD: 102773181(FADS1)
MNA: 107527686(FADS1)
HAI: 109389978 109390020(FADS1)
RSS: 109459517(FADS1)
DRO: 112317234(FADS1)
PALE: 102894313(FADS1)
LAV: 100677495
TMU: 101347278
MDO: 100028492(FADS1)
SHR: 100922163(FADS1)
PCW: 110195308(FADS1)
OAA: 103171425(FADS1)
GGA: 423119(FADS1L2) 423120(FADS1) 428851(FADS1L1)
TGU: 100225746(FADS1) 100228631
FCH: 102049758(FADS1) 106631119
CPIC: 101936861(FADS1) 101937159 101952648(FADS2)
XTR: 100489232(fads1)
NPR: 108794178(FADS1)
LCM: 102350226(FADS1)
CMK: 103174860(fads1)
FCD: 110853546
PCAN: 112557826
 » show all
Taxonomy
Reference
1  [PMID:10601301]
  Authors
Cho HP, Nakamura M, Clarke SD
  Title
Cloning, expression, and fatty acid regulation of the human delta-5 desaturase.
  Journal
J Biol Chem 274:37335-9 (1999)
DOI:10.1074/jbc.274.52.37335
  Sequence
[hsa:3992]
Reference
2  [PMID:10769175]
  Authors
Leonard AE, Kelder B, Bobik EG, Chuang LT, Parker-Barnes JM, Thurmond JM, Kroeger PE, Kopchick JJ, Huang YS, Mukerji P
  Title
cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid.
  Journal
Biochem J 347 Pt 3:719-24 (2000)
  Sequence
[hsa:3992]
Reference
3  [PMID:16403015]
  Authors
Tripodi KE, Buttigliero LV, Altabe SG, Uttaro AD
  Title
Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan.
  Journal
FEBS J 273:271-80 (2006)
DOI:10.1111/j.1742-4658.2005.05049.x
Reference
4  [PMID:21193673]
  Authors
Tavares S, Grotkjaer T, Obsen T, Haslam RP, Napier JA, Gunnarsson N
  Title
Metabolic engineering of Saccharomyces cerevisiae for production of Eicosapentaenoic Acid, using a novel {Delta}5-Desaturase from Paramecium tetraurelia.
  Journal
Appl Environ Microbiol 77:1854-61 (2011)
DOI:10.1128/AEM.01935-10
Other DBs
ExplorEnz - The Enzyme Database: 1.14.19.44
IUBMB Enzyme Nomenclature: 1.14.19.44
ExPASy - ENZYME nomenclature database: 1.14.19.44
BRENDA, the Enzyme Database: 1.14.19.44

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