Proteolytic modification of pig and rat liver pyruvate kinase including the phosphorylatable site

Bergström, Gunnel (author): Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,Engström Lorentz

Ekman, Pia (author): Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,Engström Lorentz

Humble, Elisabet (author): Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,Engström Lorentz

Engström, Lorentz (author): Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi,Engström Lorentz

(creator_code:org_t)

1978
1978
English.
In: Biochimica et Biophysica Acta. - 0006-3002 .- 1878-2434. ; 532:2, s. 259-267

Abstract Subject headings

The phosphorylated or phosphate-accepting site of pyruvate kinase from pig and rat liver was removed without inactivation by incubation with subtilisin. At different time intervals the subtilisin was inactivated with phenylmethylsulfonyl fluoride and the amount of remaining phosphorylatable or phosphorylated sites of pyruvate kinase estimated by incubation with an excess of [32P]-ATP and protein kinase. It was found that to get the same rate of modification the subtilisin concentration required to modify unphosphorylated pyruvate kinase was approximately ten times higher than that used for removal of the phosphorylated site of phosphorylated site of phosphorylated enzyme. It was shown that the proteolytically-modified pyruvate kinase had an increased apparent Km for phosphoenolpyruvate without a change in V, when compared to unmodified unphosphorylated and phosphorylated pyruvate kinase. The removal of the phosphorylated site was not associated with loss of the allosteric sites for ATP and Fru-1,6-P2. The possibility that phosphorylation of the pyruvate kinase increases its degradation rate in vivo is briefly discussed.

By the author/editor: Bergström, Gunne ...; Ekman, Pia; Humble, Elisabet; Engström, Lorent ...

About the subject

MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Basic Medicine; and Other Basic Medi ...

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