OLAH hydrolyzes decanoyl-FASN dimer to DECA and FASN dimer

Stable Identifier
Reaction [transition]
Homo sapiens
decanoyl-FASN dimer + 2 H2O => 2 decanoate + FASN dimer
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OLAH, a monomeric cytosolic thiolase, catalyzes the hydrolysis of FASN (fatty acid synthase) charged with decanoyl fatty acyl moieties to yield FASN and decanoate (DECA). OLAH expression is confined to the lactating mammary gland, and its catalytic activity enables the early termination of a portion of fatty acid biosynthesis to produce the medium chain-length fatty acids (annotated here as DECA) found in milk (Insull & Ahrens 1959; Breckenridge et al. 1969). OLAH is known only as an open reading frame identified in the human genome and as an mRNA observed in gene expression screening studies. Its biological properties are inferred from those of its well-studied rat ortholog (Libertini & Smith 1978; Mikkelsen et al. 1987).

Literature References
PubMed ID Title Journal Year
13651131 The fatty acids of human milk from mothers on diets taken ad libitum

Insull, W, Ahrens, EH

Biochem. J. 1959
5810867 Triglyceride structure of human milk fat

Kuksis, A, Marai, L, Breckenridge, WC

Can. J. Biochem. 1969
3805044 Interaction of rat mammary gland thioesterase II with fatty acid synthetase is dependent on the presence of acyl chains on the synthetase

Witkowski, A, Mikkelsen, J, Smith, S

J. Biol. Chem. 1987
627544 Purification and properties of a thioesterase from lactating rat mammary gland which modifies the product specificity of fatty acid synthetase

Libertini, LJ, Smith, S

J. Biol. Chem. 1978
Catalyst Activity

acyl-[acyl-carrier-protein] hydrolase activity of OLAH [cytosol]

Inferred From
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