Catabolism of diadenosine 5',5“'-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5',5”'-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12.

Guranowski, Andrzej; Jakubowski, Hieronim; Holler, Eggehard

doi:10.1016/s0021-9258(17)43729-x

Public

Catabolism of diadenosine 5',5“'-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5',5”'-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12.

Shared by NobleBlocks on Dec 1, 1983 • 12:00 AM UTC

Authors:

Andrzej Guranowski

Hieronim Jakubowski

Eggehard Holler

Abstract

Enzymatic activity which hydrolyzes diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) yielding ADP has been identified in extracts of eubacteria, Escherichia coli and Acidaminococcus fermentans, and of a highly thermophilic archaebacterium, Pyrodictum occultum. Specific Ap4A (symmetric) pyrophosphohydr...

Subject

Escherichia coli

Chemistry

Biochemistry

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