The Journal of the Kyushu Dental Society
Online ISSN : 1880-8719
Print ISSN : 0368-6833
ISSN-L : 0368-6833
Amino Acid and Glyoxylate Metabolism in Animal Peroxisomes
Tomoo NoguchiSatoko FujiwaraSueko Hayashi
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2003 Volume 57 Issue 4 Pages 85-93

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Abstract
Mammalian liver peroxisomes contain only one kind of aminotransferase, alanine: glyoxylate aminotransferase 1. One of the function of alanine : glyoxylate aminotransferase 1 is detoxication of glyoxylate in human. Primary hyperoxaluria type 1 is a rare autosomal recessive disease caused by a deficiency of the liver specific peroxisomal alanine : glyoxylate aminotransferase 1. Subcellular distribution, substrate specificity, response to hormone and amino acid sequence of hepatic alanine: glyoxylate aminotransferase 1 and organ distribution of the enzyme changed during rapid molecular evolution in mammals. Birds are classified into two groups on the basis of intraperoxisomal forms of liver alanine: glyoxylate aminotransferase. In the peroxisomes, alanine: glyoxylate aminotransferase was present as the holo form in guoup 1 (pigeon, sparrow, Java sparrow, Australian budgerigar, canary, goose, and duck) and as the apo form in group 2 (white leghorn, bantam, pheasant and Japanese mannikin). Physical, enzymatic and immunological properties of apo- and holo-enzymes from different birds are described.
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© 2003 The Kyushu Dental Society
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