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

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 Pseudomonas putida 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 x 10(-4) M and 5.9 x 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Raju SG,Kamath AV,Vaidyanathan CS

doi

10.1016/0006-291x(88)90173-8

subject

Has Abstract

pub_date

1988-07-29 00:00:00

pages

537-43

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(88)90173-8

journal_volume

154

pub_type

杂志文章

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