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Purification and properties of Image -mandelate-4-hydroxylase from Pseudomonas convexa

Bhat, SG and Vaidyanathan, CS (1976) Purification and properties of Image -mandelate-4-hydroxylase from Pseudomonas convexa. In: Archives of Biochemistry and Biophysics, 176 (1). pp. 314-323.

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An inducible Image -mandelate-4-hydroxylase has been partially purified from crude extracts of Pseudomonas convexa. This enzyme catalyzed the hydroxylation of Image -mandelic acid to 4-hydroxymandelic acid. It required tetrahydropteridine, NADPH, Fe2+, and O2 for its activity. The approximate molecular weight of the enzyme was assessed as 91,000 by gel filtration on Sephadex G-150. The enzyme was optimally active at pH 5.4 and 38 °C. A classical Michaelis-Menten kinetic pattern was observed with Image -mandelate, NADPH, and ferrous sulfate and Km values for these substrates were found to be 1 × 10−4, 1.9 × 10−4, and 4.7 × 10−5 Image , respectively. The enzyme is very specific for Image -mandelate as substrate. Thiol inhibitors inhibited the enzyme reaction, indicating that the sulfhydryl groups may be essential for the enzyme action. Treatment of the partially purified enzyme with denaturing agents inactivated the enzyme.

Item Type: Journal Article
Publication: Archives of Biochemistry and Biophysics
Publisher: Elservier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 10 Dec 2009 11:08
Last Modified: 19 Sep 2010 05:49
URI: http://eprints.iisc.ac.in/id/eprint/24148

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