Metabolism of DL-(+/-)-phenylalanine by Aspergillus niger.
Data(s) |
1976
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Resumo |
A fungus capable of degrading DL-phenylalanine was isolated from the soil and identified as Aspergillus niger. It was found to metabolize DL-phenylalanine by a new pathway involving 4-hydroxymandelic acid. D-Amino acid oxidase and L-phenylalanine: 2-oxoglutaric acid aminotransferase initiated the degradation of D- and L-phenylalanine, respectively. Both phenylpyruvate oxidase and phenylpyruvate decarboxylase activities could be demonstrated in the cell-free system. Phenylacetate hydroxylase, which required reduced nicotinamide adenine dinucleotide phosphate, converted phenylacetic acid to 2- and 4-hydroxyphenylacetic acid. Although 4-hydroxyphenylacetate was converted to 4-hydroxymandelate, 2-hydroxyphenylacetate was not utilized until the onset of sporulation. During sporulation, it was converted rapidly into homogentisate and oxidized to ring-cleaved products. 4-Hydroxymandelate was degraded to protocatechuate via |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/24033/1/article2.pdf Kishore, G and Sugumaran, M and Vaidyanathan, CS (1976) Metabolism of DL-(+/-)-phenylalanine by Aspergillus niger. In: Journal of Bacteriology, 128 (1). pp. 182-191. |
Publicador |
American Society for Microbiology |
Relação |
http://jb.asm.org/cgi/content/abstract/128/1/182 http://eprints.iisc.ernet.in/24033/ |
Palavras-Chave | #Biochemistry |
Tipo |
Journal Article PeerReviewed |