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Archiv für Mikrobiologie

, Volume 59, Issue 1–3, pp 4–12 | Cite as

Citramalate lyase of Clostridium tetanomorphum

  • H. A. Barker
Article

Summary

Assay methods and some properties of (+)-citramalate pyruvatelyase, an enzyme from Clostridium tetanomorphum that converts (+)-citramalate to pyruvate and acetate, are described. The enzyme is very active (0.8–1.2 units per mg protein) in freshly prepared extracts, but loses activity rapidly during storage. (+)-Citramalate is the only substrate found to be cleaved by the lyase; the equilibrium for the reaction permits almost complete cleavage at low substrate concentrations. A divalent cation is required as a cofactor. A sensitive and specific enzymic method for estimating (+)-citramalate is described.

Keywords

Enzyme Acetate Pyruvate Substrate Concentration Clostridium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1967

Authors and Affiliations

  • H. A. Barker
    • 1
  1. 1.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA

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