pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.
Ruangchan
Nantidaporn
N
Department of Biochemistry and Center of Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Rama 6 Road, Bangkok 10400, Thailand.
Tongsook
Chanakan
C
Sucharitakul
Jeerus
J
Chaiyen
Pimchai
P
D040981:Acinetobacter baumannii / Q000201:enzymology; D020134:Catalytic Domain; D004791:Enzyme Inhibitors / Q000378:metabolism / Q000494:pharmacology; D005486:Flavin Mononucleotide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006900:Hydroxylation / Q000187:drug effects; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010100:Oxygen / Q000378:metabolism; D010648:Phenylacetates / Q000378:metabolism / Q000494:pharmacology; D011550:Pseudomonas aeruginosa / Q000201:enzymology
C071365:3-hydroxyphenylacetate 6-hydroxylase; D004791:Enzyme Inhibitors; D010648:Phenylacetates; C008070:4-hydroxyphenylacetic acid; D005486:Flavin Mononucleotide; D006899:Mixed Function Oxygenases; D010100:Oxygen