The Purification and Some Properties of a Stereospecific D-asparaginase from an Extremely Thermophilic Bacterium, Thermus Aquaticus

Overview

Journal Biochem J

Specialty Biochemistry

Date 1982 Jun 1

PMID 7115316

Citations 1

Authors

G R Guy

R M Daniel

Affiliations

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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.

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PMID: 6819862 PMC: 1153914. DOI: 10.1042/bj2070641.

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