Aspartate aminotransferase of Pediococcus cerevisiae.
A five-step procedure is described for preparing highly purified aspartate aminotransferase (L-aspartate: 2-oxoglutarate aminotransferase, EC.2.6.1.1) from cell-freee enzyme extracts of Pediococcus cerevisiae. An overall purification of 130-fold was achieved. Some of P. cerevisiae aspartate aminotransferase properties were studied, i.s. pH optimum (7.8--8.0), optimum of temperature (37 degrees), Michaelis constans for 4 enzyme substrates and substrate specificity of enzyme. The enzyme is very thermolabile. During purification the enzyme was stabilizated by 2-oxoglutarate. The highly purified preparation was stored in the solution containing ammonium sulphate. The obtained aspartate aminotransferase preparation was free of alanine and aromatic amino acids aminotransferase activites and did not reveal malate dehydrogenase activity.
D001219:Aspartate Aminotransferases / Q000302:isolation & purification / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism; D002474:Cell-Free System; D004355:Drug Stability; D005971:Glutamates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007656:Ketoglutaric Acids / Q000378:metabolism; D010071:Oxaloacetates / Q000378:metabolism; D010376:Pediococcus / Q000201:enzymology*; D013696:Temperature
D005971:Glutamates; D007656:Ketoglutaric Acids; D010071:Oxaloacetates; D001224:Aspartic Acid; D001219:Aspartate Aminotransferases