Original scientific paper

Purification and Properties of Diaminopimelate Decarboxylase from Micrococcus Glutamicus

Lj. Vitale ; Department of Organic Chemistry and Biochemistry, Ruder Boskovic Institute
M. Dražić ; epartment of Organic Chemistry and Biochemistry, Ruder Boskovic Institute
M. Ladika ; epartment of Organic Chemistry and Biochemistry, Ruder Boskovic Institute

Abstract

Diaminopimelate decarboxylase (E. C. 4.1.1.20) from Micrococcus
glutamicus horn-, lysine excreting strain, is purified 350- fold by
ammonium sulphate precipitation, gel filtration on Sephadex G-150,
and chromatography on hydroxylapatite and DEAE-Seph adex. The
enzyme has a molecular weight of 53000, isoelectric point of 4.3,
optimal pH for activity 7.7, energy of activation 11.1 kcal/mol, and
Km for substrate 1.26 mM. For its stability, the presence of pyridoxal
phosphate and sulphydril reagent is necessary, and most catalytic
activity is retained within a pH range of 5.5 to 8.5. Aminoacids,
L-lysine, L-norleucine, L- u- aminoadipic, L-glutamic and L-aspartic
acid, are inhibitors of diaminopimelate decarboxylase from M.
glutamicus horn-.

Keywords

Hrčak ID:

196356

URI

https://hrcak.srce.hr/196356

Publication date:

20.7.1977.

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