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dc.contributor.authorThanawat Phongsaken_US
dc.contributor.authorJeerus Sucharitakulen_US
dc.contributor.authorKittisak Thotsapornen_US
dc.contributor.authorWorrapoj Oonananten_US
dc.contributor.authorJirundon Yuvaniyamaen_US
dc.contributor.authorJisnuson Svastien_US
dc.contributor.authorDavid P. Ballouen_US
dc.contributor.authorPimchai Chaiyenen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherChulalongkorn Universityen_US
dc.contributor.otherUniversity of Michigan, Ann Arboren_US
dc.identifier.citationJournal of Biological Chemistry. Vol.287, No.31 (2012), 26213-26222en_US
dc.description.abstractp-Hydroxyphenylacetate (HPA) 3-hydroxylase from Acinetobacter baumannii consists of a reductase component (C 1 ) and an oxygenase component (C 2 ). C 1 catalyzes the reduction of FMN by NADH to provide FMNH - as a substrate for C 2 . The rate of reduction of flavin is enhanced ∼20-fold by binding HPA. The N-terminal domain of C1 is homologous to other flavin reductases, whereas the C-terminal domain (residues 192-315) is similar to MarR, a repressor protein involved in bacterial antibiotic resistance. In this study, three forms of truncated C 1 variants and single site mutation variants of residues Arg-21, Phe-216, Arg-217, Ile-246, and Arg-247 were constructed to investigate the role of the C-terminal domain in regulating C 1 . In the absence of HPA, the C 1 variant in which residues 179-315 were removed (t178C 1 ) was reduced by NADH and released FMNH - at the same rates as wild-type enzyme carries out these functions in the presence of HPA. In contrast, variants with residues 231-315 removed behaved similarly to the wild-type enzyme. Thus, residues 179-230 are involved in repressing the production of FMNH - in the absence of HPA. These results are consistent with the C-terminal domain in the wild-type enzyme being an autoinhibitory domain that upon binding the effector HPA undergoes conformational changes to allow faster flavin reduction and release. Most of the single site variants investigated had catalytic properties similar to those of the wild-type enzyme except for the F216A variant, which had a rate of reduction that was not stimulated by HPA. F216A could be involved with HPA binding or i n the required conformational change for stimulation of flavin reduction by HPA. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleThe C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domainen_US
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