NDLI: Purification and properties of diaminopimelate decarboxylase from Micrococcus glutamicus

Content Provider	Semantic Scholar
Author	Vitale, Ljubinka
Copyright Year	1977
Abstract	Diaminopimelate decarboxylase (E. C. 4.1.1.20) from Micrococcus glutamicus horn-, lysine excreting strain, is purified 350fold by ammonium sulphate precipitation, gel filtration on Sephadex G-150, and chromatography on hydroxylapatite and DEAE-Seph adex. The enzym e h as 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, Luaminoadipic, L-glutamic and L-aspartic acid , are inhibitors of diaminopimelate decarboxylase from M. glutamicus horn-.
Starting Page	573
Ending Page	586
Page Count	14
File Format	PDF HTM / HTML
Volume Number	49
Alternate Webpage(s)	https://hrcak.srce.hr/file/289471
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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