ELOVL3,6,7 elongate PALM-CoA and Mal-CoA to 3OOD-CoA

Stable Identifier
R-HSA-548814
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
palmitoyl-CoA + malonyl-CoA => 3-oxooctadecanoyl-CoA (3-oxostearoyl-CoA) + CO2 + CoASH
ReviewStatus
5/5
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The ER membrane-bound elongation of very long chain fatty acids proteins 3, 6 and 7 (ELOVL3,6,7) catalyse the condensation of palmitoyl-CoA (PALM-CoA) with malonyl-CoA (Mal-CoA) to form 3-oxooctadecanoyl-CoA (3OOD-CoA) (Shimamura et al. 2009, Ohno et al. 2010, Naganuma et al. 2011).
Literature References
PubMed ID Title Journal Year
21959040 Biochemical characterization of the very long-chain fatty acid elongase ELOVL7

Sassa, T, Sato, Y, Ohno, Y, Kihara, A, Naganuma, T

FEBS Lett. 2011
19505953 Identification and characterization of a selective radioligand for ELOVL6

Kitazawa, H, Nagumo, A, Tang, C, Miyamoto, Y, Tokita, S, Sato, N, Nagase, T, Dean, D, Takahashi, H, Shimamura, K

J Biochem 2009
20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis

Suto, S, Sassa, T, Yamanaka, M, Igarashi, Y, Ohno, Y, Kihara, A, Mizutani, Y, Mitsutake, S

Proc Natl Acad Sci U S A 2010
Participants
Participates
Catalyst Activity

fatty acid elongase activity of ELOVL3,6,7 [endoplasmic reticulum membrane]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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