Purification and properties of 4-hydroxyphenylacetic acid 3-hydroxylase from pseudomonas putida

Raju, Satyanarayana G and Kamath, Ajith V and Vaidyanathan, CS (1988) Purification and properties of 4-hydroxyphenylacetic acid 3-hydroxylase from pseudomonas putida. In: Biochemical and Biophysical Research Communications, 154 (2). pp. 537-543.

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Abstract

4-Hydroxyphenylacetic acid 3-hydroxylase is a key enzyme in the pathway for the microbial degradation of phenylalanine, tyrosine and many aromatic amines. This enzyme was purified to homogeneity from Image by affinity chromatography. The protein had a molecular weight of 91,000 and was a dimer of identical subunits. It was a typical external flavoprotein monooxygenase and showed an absolute requirement of NADH for activity. The enzyme had a pH optimum of 7.5 and the Km values for 4-hydroxyphenylacetic acid and NADH were 2×10−4 M and 5.9×10−5 M respectively. It was strongly inhibited by heavy metal ions and thiol reagents, suggesting the possible involvement of -SH group(s) in enzyme reaction.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier science
Additional Information:	Copyright of this article belongs to Elsevier science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	16 Jan 2014 05:01
Last Modified:	16 Jan 2014 05:01
URI:	http://eprints.iisc.ac.in/id/eprint/32516

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