Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization.

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Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization.

NAD+-dependent phenylalanine dehydrogenases were purified 1,500- and 1,600-fold, and crystallized from Sporosarcina ureae SCRC-R04 and Bacillus sphaericus SCRC-R79a, respectively. The purified enzymes were homogeneous as judged by disc gel electrophoresis. The enzyme from S. ureae has a molecular weight of 305,000, while that of B. sphaericus has a molecular weight of 340,000. Each is probably ...

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Affinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System

Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...

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affinity purification and characterization of recombinant bacillus sphaericus phenylalanine dehydrogenase produced by pet expression vector system

cloning and expression of the l-phenylalanine dehydrogenase gene, from b. sphaericus in e. coli were done. the gene was cloned in the vector pet16b and transformed into e. coli bl21 (de3). the functional form of the l-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, re...

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Discrimination of aliphatic substrates by a single amino acid substitution in Bacillus badius and Bacillus sphaericus phenylalanine dehydrogenases.

Replacement of glycine by serine at positions 123 and 124 of phenylalanine dehydrogenases from Bacillus badius and Bacillus sphaericus respectively strikingly decreased enzyme activity toward aromatic amino acids and resulted in an elevation of relative activity toward aliphatic amino acids. The mutant from B. badius preferentially dehydrogenated branched-chain amino acids, while that from B. s...

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Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1987

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)61119-6