Phosphatidylcholine desaturase
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phosphatidylcholine desaturase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.19.22 | ||||||||
CAS no. | 59929-36-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a phosphatidylcholine desaturase (EC 1.14.19.22, previously EC 1.3.1.35) is an enzyme that catalyzes the chemical reaction
- 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD+ 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH + H+
Thus, the two substrates of this enzyme are 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine and NAD+, whereas its 3 products are 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine:NAD+ Delta12-oxidoreductase. Other names in common use include oleate desaturase, linoleate synthase, oleoyl-CoA desaturase, and oleoylphosphatidylcholine desaturase.
References
[edit]- Pugh EL, Kates M (March 1975). "Characterization of a membrane-bound phospholipid desaturase system of candida lipolytica". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 380 (3): 442–53. doi:10.1016/0005-2760(75)90112-5. PMID 166662.
- Slack CR, Roughan PG, Browse J (June 1979). "Evidence for an oleoyl phosphatidylcholine desaturase in microsomal preparations from cotyledons of safflower (Carthamus tinctorius) seed". The Biochemical Journal. 179 (3): 649–56. doi:10.1042/bj1790649. PMC 1186674. PMID 475773.
- Stymne S, Appelqvist LA (October 1978). "The biosynthesis of linoleate from oleoyl-CoA via oleoyl-phosphatidylcholine in microsomes of developing safflower seeds". European Journal of Biochemistry. 90 (2): 223–9. doi:10.1111/j.1432-1033.1978.tb12594.x. PMID 710426.