HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) An addition or correction has been published Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Jones, J. M. Articles by Gould, S. J. Search for Related Content PubMed PubMed Citation Articles by Jones, J. M. Articles by Gould, S. J. Social Bookmarking                      What's this?

J Biol Chem, Vol. 275, Issue 17, 12590-12597, April 28, 2000

Identification and Characterization of HAOX1, HAOX2, and HAOX3, Three Human Peroxisomal 2-Hydroxy Acid Oxidases^*

Jacob M. Jones, James C. Morrell, and Stephen J. Gould

From the Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Computer-based approaches identified three distinct human 2-hydroxy acid oxidase genes, HAOX1, HAOX2, and HAOX3, that encode proteins with significant sequence similarity to plant glycolate oxidase, a prototypical 2-hydroxy acid oxidase. The products of these genes are targeted to peroxisomes and have 2-hydroxy acid oxidase activities. Each gene displays a distinct tissue-specific pattern of expression, and each enzyme exhibits distinct substrate preferences. HAOX1 is expressed primarily in liver and pancreas and is most active on the two-carbon substrate, glycolate, but is also active on 2-hydroxy fatty acids. HAOX2 is expressed predominantly in liver and kidney and displays highest activity toward 2-hydroxypalmitate. HAOX3 expression was detected only in pancreas, and this enzyme displayed a preference for the medium chain substrate 2-hydroxyoctanoate. These results indicate that all three human 2-hydroxy acid oxidases are involved in the oxidation of 2-hydroxy fatty acids and may also contribute to the general pathway of fatty acid -oxidation. Primary hyperoxaluria type 1 (PH1) is caused by defects in peroxisomal alanine-glyoxylate aminotransferase, the enzyme that normally eliminates intraperoxisomal glyoxylate. The presence of HAOX1 in liver and kidney peroxisomes and the ability of HAOX1 to oxidize glyoxylate to oxalate implicate HAOX1 as a mediator of PH1 pathophysiology.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				V. Foulon, M. Sniekers, E. Huysmans, S. Asselberghs, V. Mahieu, G. P. Mannaerts, P. P. Van Veldhoven, and M. Casteels Breakdown of 2-Hydroxylated Straight Chain Fatty Acids via Peroxisomal 2-Hydroxyphytanoyl-CoA Lyase: A REVISED PATHWAY FOR THE {alpha}-OXIDATION OF STRAIGHT CHAIN FATTY ACIDS J. Biol. Chem., March 18, 2005; 280(11): 9802 - 9812. [Abstract] [Full Text] [PDF]

				K. J. Wallace, R. H. Wallis, S. C. Collins, K. Argoud, P. J. Kaisaki, A. Ktorza, P. Y. Woon, M.-T. Bihoreau, and D. Gauguier Quantitative trait locus dissection in congenic strains of the Goto-Kakizaki rat identifies a region conserved with diabetes loci in human chromosome 1q Physiol Genomics, September 16, 2004; 19(1): 1 - 10. [Abstract] [Full Text] [PDF]

				S. Reumann, C. Ma, S. Lemke, and L. Babujee AraPerox. A Database of Putative Arabidopsis Proteins from Plant Peroxisomes Plant Physiology, September 1, 2004; 136(1): 2587 - 2608. [Abstract] [Full Text] [PDF]

				G. Dodt, D. Warren, E. Becker, P. Rehling, and S. J. Gould Domain Mapping of Human PEX5 Reveals Functional and Structural Similarities to Saccharomyces cerevisiae Pex18p and Pex21p J. Biol. Chem., November 2, 2001; 276(45): 41769 - 41781. [Abstract] [Full Text] [PDF]

				J. M. Jones, J. C. Morrell, and S. J. Gould Multiple Distinct Targeting Signals in Integral Peroxisomal Membrane Proteins J. Cell Biol., June 4, 2001; 153(6): 1141 - 1150. [Abstract] [Full Text] [PDF]