Purification and properties of 4-hydroxyphenylacetic acid 3-hydroxylase from pseudomonas putida
Data(s) |
29/07/1988
|
---|---|
Resumo |
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. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/32516/1/purification.pdf 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. |
Publicador |
Elsevier science |
Relação |
http://dx.doi.org/10.1016/0006-291X(88)90173-8 http://eprints.iisc.ernet.in/32516/ |
Palavras-Chave | #Biochemistry |
Tipo |
Journal Article PeerReviewed |