Kittisak ThotsapornJeerus SucharitakulJanewit WongratanaChutintorn SuadeePimchai ChaiyenMahidol University2018-07-242018-07-242004-10-05Biochimica et Biophysica Acta - Gene Structure and Expression. Vol.1680, No.1 (2004), 60-66016747812-s2.0-4644255461https://repository.li.mahidol.ac.th/handle/20.500.14594/21143The genes encoding for the reductase and oxygenase components of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii were cloned and expressed in an E. coli system. The recombinant enzymes were purified and shown to have the same catalytic properties as the native enzyme. Sequence analysis and biochemical studies indicate that the enzyme represents a novel prototype of enzyme in the two-protein component class of aromatic hydroxylases. The C2component shows little similarity to other oxygenases in the same class, correlating with its uniquely broad flavin specificity. Analysis of the C1reductase sequence indicates that the binding sites of flavin and NADH mainly reside in the N-terminal half while the C-terminal half may be responsible for HPA-stimulation of NADH oxidation. © 2004 Elsevier B.V. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/j.bbaexp.2004.08.003