Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species
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چکیده
منابع مشابه
Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.
D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, Bacillus sp. YM-1, which was newly isolated from a sauna dust. The enzyme has a molecular weight of about 62,000 and consists of two subunits identical in molecular weight (30,000). It catalyzes transamination between various D-amino acids and alpha-keto acids, al...
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The gene for thermostable D-amino acid aminotransferase from a thermophile, Bacillus species YM-1 was cloned and expressed efficiently in Escherichia coli. The entire covalent structure of the enzyme was determined from the nucleotide sequence of the cloned gene and mostly confirmed by amino acid sequences of tryptic peptides from the gene product. The polypeptide is composed of 282 amino acid ...
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Isolation and identification of thermophilic Bacillus sp was carried out from a soil sample. The cells were cultivated in a medium containing soluble starch as sole carbon source. The addition of calcium (10 mM) or peptone (1%) and yeast extract (0.5%) to the medium shortened the lag period and improved the growth and amylase synthesis. The optimum temperature for amylase production was detecte...
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متن کاملThermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.
The gene encoding aspartate aminotransferase of a thermophilic Bacillus species, YM-2, has been cloned and expressed efficiently in Escherichia coli. The primary structure of the enzyme was deduced from nucleotide sequences of the gene and confirmed mostly by amino acid sequences of tryptic peptides. The gene consists of 1,176 base pairs encoding a protein of 392 amino acid residues; the molecu...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81633-2