Publication:
Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: Evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases

1

Issued Date

2004-10-05

Resource Type

Article

ISSN

01674781

DOI

10.1016/j.bbaexp.2004.08.003

Other identifier(s)

2-s2.0-4644255461

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Biochimica et Biophysica Acta - Gene Structure and Expression. Vol.1680, No.1 (2004), 60-66

Suggested Citation

Kittisak Thotsaporn, Jeerus Sucharitakul, Janewit Wongratana, Chutintorn Suadee, Pimchai Chaiyen Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: Evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases. Biochimica et Biophysica Acta - Gene Structure and Expression. Vol.1680, No.1 (2004), 60-66. doi:10.1016/j.bbaexp.2004.08.003 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/21143

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Title

Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: Evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases

Author(s)

Kittisak Thotsaporn
 Jeerus Sucharitakul
 Janewit Wongratana
 Chutintorn Suadee
 Pimchai Chaiyen

Other Contributor(s)

Mahidol University

Abstract

The 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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

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URI

https://repository.li.mahidol.ac.th/handle/123456789/21143

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Scopus 2001-2005