Metabolism of DL-(+/-)-phenylalanine by Aspergillus niger.

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.

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Abstract

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

Item Type:	Journal Article
Publication:	Journal of Bacteriology
Publisher:	American Society for Microbiology
Additional Information:	Copyright of this article belongs to American Society for Microbiology.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	11 Dec 2009 06:24
Last Modified:	19 Sep 2010 05:48
URI:	http://eprints.iisc.ac.in/id/eprint/24033

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