Acyl-CoA synthetase catalyzes the synthesis of diadenosine hexaphosphate (Ap6A)

被引：13

作者：

Fontes, R

Sillero, MAG

Sillero, A

机构：

[1] UAM, Fac Med, Dept Bioquim, CSIC,Inst Invest Biomed Alberto Sols, Madrid 28029, Spain

[2] Univ Porto, Fac Med, Serv Quim Fisiol, P-4100 Porto, Portugal

来源：

BIOCHIMIE | 1999年 / 81卷 / 03期

关键词：

diadenosine hexaphosphate; diadenosine pentaphosphate; dinucleoside polyphosphates; acyt-CoA synthetase; Pseudomonas fragi;

D O I：

10.1016/S0300-9084(99)80056-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：229 / 233

页数：5

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