Previous Article | Next Article ![]()
Journal of Bacteriology, November 2005, p. 7696-7702, Vol. 187, No. 22
0021-9193/05/$08.00+0 doi:10.1128/JB.187.22.7696-7702.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Programme in Environmental Microbiology, Department of Microbiology, National University of Singapore, Singapore,1 Department of Biotechnology, Malaysia University of Science and Technology, 47301 Petaling Jaya, Malaysia,2 School of Biomedical Science, Curtin University of Technology, Bentley, Australia3
Received 20 March 2005/ Accepted 26 August 2005
The xlnD gene from Pseudomonas alcaligenes NCIMB 9867 (strain P25X) was shown to encode 3-hydroxybenzoate 6-hydroxylase I, the enzyme that catalyzes the NADH-dependent conversion of 3-hydroxybenzoate to gentisate. Active recombinant XlnD was purified as a hexahistidine fusion protein from Escherichia coli, had an estimated molecular mass of 130 kDa, and is probably a trimeric protein with a subunit mass of 43 kDa. This is in contrast to the monomeric nature of the few 3-hydroxybenzoate 6-hydroxylases that have been characterized thus far. Like other 3-hydroxybenzoate 6-hydroxylases, XlnD could utilize either NADH or NADPH as the electron donor. P25X harbors a second 3-hydroxybenzoate 6-hydroxylase II that was strictly inducible by specific aromatic substrates. However, the degradation of 2,5-xylenol and 3,5-xylenol in strain P25X was found to be dependent on the xlnD-encoded 6-hydroxylase I and not the second, strictly inducible 6-hydroxylase II.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»