Purification and crystallization of D-amino acid aminotransferase ofBacillus sphaericus
نویسندگان
چکیده
منابع مشابه
D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties.
D-Amino acid aminotransferase, purified to homogeneity and crystallized from Bacillus sphaericus, has a molecular weight of about 60,000 and consists of two subunits identical in molecular weight (30,000). The enzyme exhibits absorption maxima at 280, 330, and 415 nm, which are independent of the pH (5.5 to 10.0), and contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme. One of the pyrido...
متن کاملBranched Chain Amino Acid Aminotransferase
The kinetics of transamination reactions catalyzed by pig heart “branched chain amino acid” aminotransferase was investigated. The activation of aged preparations by 2mercaptoethanol, previously noted, was associated with increases in both the maximum velocity and enzyme-substrate affinities. This implies a protein conformational change. The sharp pH optimum observed with standard assay conditi...
متن کاملThermostable 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...
متن کاملPurification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.
The branched chain amino acid aminotransferase [EC 2.6.1.42] was purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. The enzyme had a molecular weight of about 93,000 and consisted of two identical subunits, each with a molecular weight of about 47,000. One pyridoxal phosphate is bound per subunit. In addition to branched chain amino acids, the enzyme uses L...
متن کاملAspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1974
ISSN: 0014-5793
DOI: 10.1016/0014-5793(74)80407-2