Abstract
Pyruvate (glyoxylate) aminotransferase from rat liver peroxisomes was highly purified and characterized. The enzyme preparation has a mol.wt. of approx. 80,000 with two identical subunits, and isoelectric point of 8.0 and a pH optimum between 8.0 and 8.5. The enzyme catalysed transamination between a number of L-amino acids and pyruvate or glyoxylate. The effective amino acceptors were pyruvate, phenylpyruvate and glyoxylate with serine, and glyoxylate and phenylpyruvate with alanine as amino donor. These properties and kinetic parameters of the enzyme are remarkably similar to those previously described for mitochondrial alanine-glyoxylate aminotransferase isoenzyme 1 from glucagon-injected rat liver [Noguchi, Okuno, Takada, Minatogawa, Okai & Kido (1978, Biochem. J. 169, 113-122].
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- Cooper A. J. Asparagine transaminase from rat liver. J Biol Chem. 1977 Mar 25;252(6):2032–2038. [PubMed] [Google Scholar]
- Cooper A. J., Meister A. Isolation and properties of a new glutamine transaminase from rat kidney. J Biol Chem. 1974 Apr 25;249(8):2554–2561. [PubMed] [Google Scholar]
- Hsieh B., Tolbert N. E. Glyoxylate aminotransferase in peroxisomes from rat liver and kidney. J Biol Chem. 1976 Jul 25;251(14):4408–4415. [PubMed] [Google Scholar]
- Noguchi T., Minatogawa Y., Takada Y., Okuno E., Kido R. Subcellular distribution of pyruvate (glyoxylate) aminotransferases in rat liver. Biochem J. 1978 Jan 15;170(1):173–175. doi: 10.1042/bj1700173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noguchi T., Okuno E., Kido R. Identity of isoenzyme 1 of histidine-pyruvate aminotransferase with serine-pyruvate aminotransferase. Biochem J. 1976 Dec 1;159(3):607–613. doi: 10.1042/bj1590607. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noguchi T., Okuno E., Kido R. Identity of rat kidney histidine-pyruvate aminotransferase with glutamine-oxo acid aminotransferase. Biochem J. 1977 Jan 1;161(1):177–179. doi: 10.1042/bj1610177. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noguchi T., Okuno E., Minatogawa Y., Kido R. Purification, characterization and identification of rat liver histidine-pyruvate aminotransferase isoenzymes. Biochem J. 1976 Apr 1;155(1):107–115. doi: 10.1042/bj1550107. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noguchi T., Okuno E., Takada Y., Minatogawa Y., Okai K., Kido R. Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species. Biochem J. 1978 Jan 1;169(1):113–122. doi: 10.1042/bj1690113. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Noguchi T., Takada Y., Kido R. Characteristics of hepatic serine-pyruvate aminotransferase in different mammalian species. Biochem J. 1977 Mar 1;161(3):609–614. doi: 10.1042/bj1610609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rowsell E. V., Snell K., Carnie J. A., Rowsell K. V. The subcellular distribution of rat liver L-alanine-glyoxylate aminotransferase in relation to a pathway for glucose formation involving glyoxylate. Biochem J. 1972 Mar;127(1):155–165. doi: 10.1042/bj1270155. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Snell K., Walker D. G. Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat. Biochem J. 1974 Dec;144(3):519–531. doi: 10.1042/bj1440519. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Snell K., Walker D. G. The adaptive behaviour of isoenzyme forms of rat liver alanine aminotransferases during development. Biochem J. 1972 Jun;128(2):403–413. doi: 10.1042/bj1280403. [DOI] [PMC free article] [PubMed] [Google Scholar]