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Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase.

Authors: Suematsu, N  Okamoto, K  Shibata, K  Nakanishi, Y  Isohashi, F 
Citation: Suematsu N, etal., Eur J Biochem 2001 May;268(9):2700-9.
Pubmed: (View Article at PubMed) PMID:11322891

A cytosolic acetyl-CoA hydrolase (CACH) was purified from rat liver to homogeneity by a new method using Triton X-100 as a stabilizer. We digested the purified enzyme with an endopeptidase and determined the N-terminal amino-acid sequences of the two proteolytic fragments. From the sequence data, we designed probes for RT-PCR, and amplified CACH cDNA from rat liver mRNA. The CACH cDNA contains a 1668-bp ORF encoding a protein of 556 amino-acid residues (62 017 Da). Recombinant expression of the cDNA in insect cells resulted in overproduction of functional acetyl-CoA hydrolase with comparable acyl-CoA chain-length specificity and Michaelis constant for acetyl-CoA to those of the native CACH. Database searching shows no homology to other known proteins, but reveals high similarities to two mouse expressed sequence tags (91% and 93% homology) and human mRNA for KIAA0707 hypothetical protein (50% homology) of unknown function.


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RGD Object Information
RGD ID: 633789
Created: 2003-08-29
Species: All species
Last Modified: 2004-05-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.