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Studies on a 2, 3-diaminopropionate: Ammonia-lyase from a pseudomonad.

Vijayalakshmi, K. R. and Rajagopal Rao, D. and Raghavendra Rao, M. R. (1975) Studies on a 2, 3-diaminopropionate: Ammonia-lyase from a pseudomonad. Hoppe Seyler's Zeitschrift fuer Physiologische Chemie, 356. pp. 193-201.

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Abstract

2,3-Diaminopropionate:ammonia-lyase, an induced enzyme in a Pseudomonas isolate, has been purified 40-fold and found to be homogeneous by disc gel electrophoresis and by ultracentrifugation. Some of its properties have been studied. The optimum pH and temperature for activity are 8 and 40 degree c, respectively. The enzyme shows a high degree of substrate specificity, acting only on 2,3-diaminopropionate; the D-isomer is only one-eighth as effective as the L-form. L-Homoserine and DL-cystathionine are not substrates, and 3-cyanoalanine does not inhibit its activity. It is a pyridoxal phosphate enzyme which requires free enzyme sulphhydryls for activity. The Kmvalues for L-2,3-diaminopropionate and pyridoxal phosphate are 1mM and 25uM, respectively. The molecular weight of the enzyme is about 80000 as determined by gel ftltration. On treatment with 0.5M urea or guanidine hydrochloride, the enzyme dissociates into inactive subunits with an approximate molecular weight of 45000. One mole of the active enzyme binds one mole of pyridoxal phosphate. The bacterial enzyme seems to be quite different in many of its properties from the rat liver enzyme which also exhibits the substrate specificity of cystathionine lyase.

Item Type: Article
Uncontrolled Keywords: Pseudomonas, 2,3-Diaminopropionate ammonia lyase, induced enzyme
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 13 Jul 2016 10:51
Last Modified: 13 Jul 2016 10:51
URI: http://ir.cftri.com/id/eprint/5563

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