The purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus.
Ontology highlight
ABSTRACT: 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.
SUBMITTER: Guy GR
PROVIDER: S-EPMC1158297 | biostudies-other | 1982 Jun
REPOSITORIES: biostudies-other
ACCESS DATA