D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties.
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 کاملProperties of meso - a , € - Diaminopimelate D - Dehydrogenase from Bacillus sphaericus
meso-a,eDiaminopimelate D-dehydrogenase, which has been purified to homogeneity from the extract of Bacillus sphaericus IF0 3626, has a molecular weight of about 80,000 and consists of two subunits identical in molecular weight (approximately 40,000). The enzyme has a high substrate specificity. In addition to mso-a,diaminopimelate, lanthionine is deaminated by the enzyme to a far lesser extent...
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 کاملEffects of salts on the conformation and catalytic properties of d-amino acid aminotransferase.
The effects of salts on the biochemical properties of D-amino acid aminotransferase from Bacillus sp. YM-1 have been studied to elucidate both the inhibitory effects of salts on the activity and the protective effects of salts on the substrate-induced inactivation. The results from UV-visible spectroscopy studies on the reaction of the enzyme with D-serine revealed that salt significantly reduc...
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 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: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41029-6