GTPase-mediated activation of ATP sulfurylase.
J Biol Chem
; 267(1): 542-5, 1992 Jan 05.
Article
en En
| MEDLINE
| ID: mdl-1730615
GTP stimulates the synthesis of APS (adenosine 5'-phosphosulfate) by the enzyme ATP sulfurylase (ATP:sulfate adenylyltransferase, EC 2.7.7.4) via a GTPase mechanism. The activation of the enzyme, purified from Escherichia coli, is titratable with GTP. The initial rate of APS formation is increased 116-fold at a saturating concentration of GTP. The enzyme exhibits a GTPase activity that is stimulated by ATP and further enhanced by SO4; however, SO4 alone does not significantly stimulate GTP hydrolysis. The larger subunit of ATP sulfurylase, encoded by cysN, contains a GTP-binding consensus sequence common to other known GTP-binding proteins. This is the first evidence that the sulfate activation pathway is a metabolic target for regulation by a GTPase.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sulfato Adenililtransferasa
/
GTP Fosfohidrolasas
Idioma:
En
Revista:
J Biol Chem
Año:
1992
Tipo del documento:
Article
Pais de publicación:
Estados Unidos