Conserved Site

Fatty acid desaturase, type 1, C-terminal (IPR001522)

Short name: Fatty_acid_desaturase-1_C


Fatty acid desaturases are enzymes that catalyse the insertion of a double bond at the delta position of fatty acids.

There seems to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: the first contains stearoyl-CoA desaturase (SCD) (EC:; the second includes plant stearoyl-acyl-carrier protein and cyanobacteria desA protein.

SCD is a key regulatory enzyme of unsaturated fatty acid biosynthesis. In association with cytochrome b5 and NADP-dependent cytochrome b5 reductase, it constitutes part of a microsomal membrane-bound 3-component system in animals and fungi [PMID: 2903162]. SCD contains 4 putative transmembrane (TM) regions that anchor it in the microsomal membrane. SCD uses oxygen and electrons from reduced cytochrome b5 [PMID: 1978720,PMID: 2428815] to catalyse the insertion of a cis double bond between carbons 9 and 10 of a spectrum of fatty acids [PMID: 2903162,PMID: 1978720,PMID: 2428815]. The preferred substrates of SCD are palmitoyl-CoA and stearoyl-CoA, which are converted to palmitoleic (16:1) and oleic (18:1) acids respectively [PMID: 2903162,PMID: 2428815]. These unsaturated molecules are the major storage form of fatty acids (as triacylglycerols) in adipocytes [PMID: 2903162].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns