Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1979 Aug;64(2):176–181. doi: 10.1104/pp.64.2.176

Conversion of l- and d-Phenylalanine to Phenylacetate via Phenylpyruvate in Sorghum Leaf Extracts 1

Helen A Stafford a, Leslie L Lewis a
PMCID: PMC543049  PMID: 16660927

Abstract

The incorporation of dl-[14C]phenylalanine into phenylacetate reported previously in leaf enzyme preparations has been found to be catalyzed by two separate enzyme activities leading to phenylpyruvate, one using the l-, the other the d-isomer. Since both reactions occur anaerobically and are increased by the addition of pyridoxal phosphate and α-ketoglutarate, two transaminase (aminotransferase) activities appear to be involved. The activities of the l- and d-dependent forms are approximately equal in a crude particulate fraction, but range from 1:1 to 3:1 in a soluble supernatant fraction. Nonisotopic as well as isotopic assays to separate d- and l-activities are described.

Full text

PDF
176

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Forest J. C., Wightman F. Amino acid metabolism in plants. 3. Purification and some properties of a multispecific aminotransferase isolated from bushbean seedlings (Phaseolus vulgaris L.). Can J Biochem. 1972 Jul;50(7):813–829. doi: 10.1139/o72-113. [DOI] [PubMed] [Google Scholar]
  2. Havir E. A., Hanson K. R. L-phenylalanine ammonia-lyase. II. Mechanism and kinetic properties of the enzyme from potato tubers. Biochemistry. 1968 May;7(5):1904–1914. doi: 10.1021/bi00845a039. [DOI] [PubMed] [Google Scholar]
  3. Jack G. W., McMahon P. C. A bacterial phenylalanine aminotransferase lacking pyridoxal 5'-phosphate as cofactor. Biochim Biophys Acta. 1978 Apr 12;523(2):344–357. doi: 10.1016/0005-2744(78)90037-2. [DOI] [PubMed] [Google Scholar]
  4. Miura G. A., Mills S. E. The Conversion of d-Tryptophan to l-Tryptophan in Cell Cultures of Tobacco. Plant Physiol. 1971 Apr;47(4):483–487. doi: 10.1104/pp.47.4.483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ogawa T., Fukuda M., Sasaoka K. Occurrence of D-amino acid aminotransferase in pea seedlings. Biochem Biophys Res Commun. 1973 Jun 8;52(3):998–1002. doi: 10.1016/0006-291x(73)91036-x. [DOI] [PubMed] [Google Scholar]
  6. Riddle V. M., Mazelis M. Conversion of Tryptophan to Indoleacetamide and Further Conversion to Indoleacetic Acid by Plant Preparations. Plant Physiol. 1965 May;40(3):481–484. doi: 10.1104/pp.40.3.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Stafford H. A., Lewis L. L. Interference by a phenylacetate pathway in isotopic assays for phenylalanine ammonia-lyase in leaf extracts. Plant Physiol. 1977 Dec;60(6):830–834. doi: 10.1104/pp.60.6.830. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES