Literature summary for 2.3.1.75 extracted from

Kawelke, S.; Feussner, I.
Two predicted transmembrane domains exclude very long chain fatty acyl-CoAs from the active site of mouse wax synthase (2015), PLoS ONE, 10, e0145797.

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Protein Variants

Protein Variants	Comment	Organism
additional information	domain swap experiment between the mouse acyl-CoA:wax alcohol acyltransferase (AWAT2) and the homologous mouse acyl-CoA:diacylglycerol O-acyltransferase 2 (DGAT2). Te substrate specificity of AWAT2 is partially determined by two predicted transmembrane domains near the amino terminus of AWAT2. Upon exchange of the two domains for the respective part of DGAT2, the resulting chimeric enzyme is capable of incorporating up to 20% of very long acyl chains in the wax esters upon expression in Saccharomyces cerevisiae. The amount of very long acyl chains in wax esters synthesized by wild type AWAT2 is negligible. The effect is due to a single amino acid exchange within one of the predicted membrane domains, the AWAT2 N36R	Mus musculus
N36R	mutant enzyme is capable of synthesizing very long chain fatty acyl-harboring wax esters	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q6E1M8	-	-

Synonyms

Synonyms	Comment	Organism
AWAT2	-	Mus musculus

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Release 2023.1 (January 2023)