Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase fromRhodobacter sphaeroidesOU5-Reference-Cited by-同舟云学术

Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase fromRhodobacter sphaeroidesOU5

Published:2008-10 Issue:10 Volume:54 Page:829-834
ISSN:0008-4166
Container-title:Canadian Journal of Microbiology
language:en
Short-container-title:Can. J. Microbiol.

Author:

Ranjith N. K.¹²,Ramana Ch. V.¹²,Sasikala Ch.¹²

Affiliation:

1. Department of Plant Sciences, School of Life Sciences, University of Hyderabad, P.O. Central University, Hyderabad 500 046, India.

2. Bacterial Discovery Laboratory, Center for Environment, IST, JNT University, Kukatpally, Hyderabad 500 085, India.

Abstract

An enzyme involved in the catabolism of 3,4-dihydroxyphenylalanine (DOPA) was isolated from Rhodobacter sphaeroides OU5. The enzyme catalyzes the formation of 3,4-dihydroxyphenylpyruvic acid (DOPP) and ammonia from DOPA. Formation of ammonia by DOPA oxidative deaminase was O2dependent and the enzyme isolated to its homogeneity has 100% affinity for DOPA. DOPA oxidative deaminase is functional at low concentrations of the substrate (<100 μmol·L–1) and is independent of NADH. The molecular mass of the purified enzyme is ~190 kDa and the enzyme could be a pentamer of 54, 42, 34, 25, and 23 kDa subunits as determined by SDS–PAGE.

Publisher

Canadian Science Publishing

Subject

Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology

Link

http://www.nrcresearchpress.com/doi/pdf/10.1139/W08-071

Reference14 articles.

1. Amino Acid Degradation by Anaerobic Bacteria

2. Mutation of Tyrosine 332 to Phenylalanine Converts Dopa Decarboxylase into a Decarboxylation-dependent Oxidative Deaminase

3. Biebl, H., and Pfennig, N. 1981. Isolation of members of the family Rhodospirillaceae.InThe prokaryotes.Edited byM.P. Starr, H. Stolp, H.G. Truper, A. Balows, and H.G. Schlegel. Springer-Verlag, New York. pp. 167–273.

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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