Raju, Satyanarayana G. ; Kamath, Ajith V. ; Vaidyanathan, C. S. (1988) Purification and properties of 4-hydroxyphenylacetic acid 3-hydroxylase from Pseudomonas putida Biochemical and Biophysical Research Communications, 154 (2). pp. 537-543. ISSN 0006-291X
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Official URL: http://www.sciencedirect.com/science/article/pii/0...
Related URL: http://dx.doi.org/10.1016/0006-291X(88)90173-8
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 ρH 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.
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