Arginine Racemase of Pseudomonas graveolens
نویسندگان
چکیده
منابع مشابه
Arginine racemase of Pseudomonas graveolens. II. Racemization and transamination of ornithine catalyzed by arginine racemase.
Arginine racemase from Pseudomonas graveolens is inactivated by preliminary incubation with Lor D-ornithine, 6-Nacetyl-L-ornithine, and L-2,4-diaminobutyrate at pH 10.0. Loss of the enzyme activity is associated with formation of a new spectrum with an absorption maximum in the region of 320 rnp and disappearance of a peak at 420 mp. The inactivation is prevented, and the inactivated enzyme is ...
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Arginine biosynthesis in Pseudoinonas aeruginosa proceeded via transacetylation of acetylornithine with glutamate ; it resembled Micrococcus glutamicus rather than Escherichia coli. Of four arginine biosynthetic enzymes, N-acetyl-y-glutamokinase, N-acetylornithine glutamate transacetylase, ornithine transcarbamylase and argininosuccinase determined under various conditions of arginine excess an...
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Non-pigmented strains of Pseudomonas pyocyanea occur frequently and this organism has only limited activity in conventional biochemical tests; 50 strains were tested for the presence of arginine dihydrolase and found positive whereas only Salmonella sp. and Enterobacter sp. among other Gram-negative species were positive. The test for arginine dihydrolase is rapid and simple and suitable for ro...
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An arginine decarboxylase has been isolated from a Pseudomonas species. The enzyme is constitutive and did not appear to be repressed by a variety of carbon sources. After an approximately 40-fold purification, the enzyme appeared more similar in its properties to the Escherichia coli biosynthetic arginine decarboxylase than to the E. coli inducible (biodegradative) enzyme. The Pseudomonas argi...
متن کاملEvidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase.
A positively charged residue, R219, was found to interact with the pyridine nitrogen of pyridoxal phosphate in the structure of alanine racemase from Bacillus stearothermophilus [Shaw et al. (1997) Biochemistry 36, 1329-1342]. Three site-directed mutants, R219K, R219A, and R219E, have been characterized and compared to the wild type enzyme (WT) to investigate the role of R219 in catalysis. The ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61972-6