The purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus.
A specific D-asparaginase was isolated and crystallized from Thermus aquaticus strain T351. It is present in larger amounts than the L-asparaginase. The enzyme has a molecular weight of 60 000, an isoelectric point of 4.8 and a Km of 2 mM. It has 6 disulphide bonds/molecule, and a histidine residue at the active site. It is inhibited by keto acids and by high salt concentrations.
D001215:Asparaginase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D001216:Asparagine / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D013237:Stereoisomerism; D013696:Temperature; D013824:Thermus / Q000201:enzymology*
D001216:Asparagine; D001215:Asparaginase