Conversion of l- and d-Phenylalanine to Phenylacetate via Phenylpyruvate in Sorghum Leaf Extracts 1
AUTOR(ES)
Stafford, Helen A.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=543049Documentos Relacionados
- Amino Acid Isomerization in the Production of l-Phenylalanine from d-Phenylalanine by Bacteria1
- Chiral discrimination in cyclodextrin complexes of amino acid derivatives: β-cyclodextrin/ N-acetyl-l-phenylalanine and N-acetyl- d-phenylalanine complexes
- Highly potent analogues of luteinizing hormone-releasing hormone containing D-phenylalanine nitrogen mustard in position 6.
- Interference by a Phenylacetate Pathway in Isotopic Assays for Phenylalanine Ammonia-Lyase in Leaf Extracts 1
- Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates.
