Your browser version may not work well with NCBI's Web applications. More information here...
1: Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8.Click here to read Links

Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase.

Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T.

Department of Biochemistry, Shinshu University School of Medicine, Nagano, Japan.

cDNA encoding the human peroxisomal acyl-coenzyme A oxidase (AOX) was cloned and sequenced. The longest cDNA insert isolated has 3083 bases and encodes the entire protein of 661-amino acids, including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal. At the amino acid level, the significantly high homology (89%) to rat AOX was found. In the cDNA-expression experiment, significant amount of AOX was accumulated in human skin fibroblast and the expressed AOX was catalytically active, while only a limited amount was found in Zellweger syndrome patient's fibroblast not having normal peroxisomes.

PMID: 8117268 [PubMed - indexed for MEDLINE]