Acyl-CoA synthetase catalyzes the synthesis of diadenosine hexaphosphate (Ap(6)A)

• Type: Article in International Scientific Journal
• Date: 1999

Authors

fontes, r (Author) FMUP; sillero, mag (Author) Other; sillero, a (Author) Other

Journal

Title: Biochimie

Vol. 81

Pages: 229-233

ISSN: 0300-9084

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 13 Citations

Scopus - 10 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-001-4XR

DOI: 10.1016/s0300-9084(99)80056-x

Abstract (EN): The synthesis of diadenosine hexaphosphate (Ap(6)A), a potent vasoconstrictor, is catalyzed by acyl-CoA synthetase from Pseudomonas fragi. In a first step AMP is transferred from ATP to tetrapolyphosphate (P-4) originating adenosine pentaphosphate (p(5)A) which, subsequently, is the acceptor of another AMP moiety from ATP generating diadenosine hexaphosphate (Ap(6)A). Diadenosine pentaphosphate (Ap(5)A) and diadenosine tetraphosphate (Ap(4)A) were also synthesized in the course of the reaction. In view of the variety of biological effects described for these compounds the potential capacity of synthesis of diadenosine polyphosphates by the mammalian acyl-CoA synthetases may be relevant, (C) Societe francaise de biochimie et biologic moleculaire / Elsevier, Paris.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5