HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Powlowski, J. B. Articles by Ballou, D. P. Search for Related Content PubMed PubMed Citation Articles by Powlowski, J. B. Articles by Ballou, D. P. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 262, Issue 1, 69-74, Jan, 1987

Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum

JB Powlowski, S Dagley, V Massey and DP Ballou

Anthranilate hydroxylase was purified from the yeast Trichosporon cutaneum. This enzyme is a simple flavoprotein which apparently does not require any additional cofactor for the conversion of anthranilate to 2,3-dihydroxybenzoate. Anthranilate hydroxylase has Mr of approximately 95,000, with subunit Mr of 50,000; it contains 2 mol of FAD/mol of enzyme. A number of compounds in addition to anthranilate serve as substrates, or effectors, for this enzyme. Oxygen-labeling experiments show that the oxygen atom at the 3-position of the product, 2,3-dihydroxybenzoate, originates from O2, while that at the 2-position is derived from H2O. A mechanism is proposed involving imine formation and hydrolysis during the reaction with the flavin hydroperoxide formed from reduced enzyme flavin and molecular oxygen. This proposal is in accord with the mechanism postulated for other flavoprotein aromatic hydroxylases.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H.-K. Chang, P. Mohseni, and G. J. Zylstra Characterization and Regulation of the Genes for a Novel Anthranilate 1,2-Dioxygenase from Burkholderia cepacia DBO1 J. Bacteriol., October 1, 2003; 185(19): 5871 - 5881. [Abstract] [Full Text] [PDF]

				S. Chakraborty and V. Massey Reaction of Reduced Flavins and Flavoproteins with Diphenyliodonium Chloride J. Biol. Chem., October 25, 2002; 277(44): 41507 - 41516. [Abstract] [Full Text] [PDF]

				M. E.-S. Mohamed, A. Zaar, C. Ebenau-Jehle, and G. Fuchs Reinvestigation of a New Type of Aerobic Benzoate Metabolism in the Proteobacterium Azoarcus evansii J. Bacteriol., March 15, 2001; 183(6): 1899 - 1908. [Abstract] [Full Text]

				D. M. Eby, Z. M. Beharry, E. D. Coulter, D. M. Kurtz Jr., and E. L. Neidle Characterization and Evolution of Anthranilate 1,2-Dioxygenase from Acinetobacter sp. Strain ADP1 J. Bacteriol., January 1, 2001; 183(1): 109 - 118. [Abstract] [Full Text]

				B. M. Bundy, A. L. Campbell, and E. L. Neidle Similarities between the antABC-Encoded Anthranilate Dioxygenase and the benABC-Encoded Benzoate Dioxygenase of Acinetobacter sp. Strain ADP1 J. Bacteriol., September 1, 1998; 180(17): 4466 - 4474. [Abstract] [Full Text]