PMID:1730615
| Citation |
Leyh, TS and Suo, Y (1992) GTPase-mediated activation of ATP sulfurylase. J. Biol. Chem. 267:542-5 |
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| Abstract |
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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| Keywords |
Amino Acid Sequence; Binding Sites; Electrophoresis, Gel, Two-Dimensional; Enzyme Activation; Escherichia coli/enzymology; GTP Phosphohydrolases/metabolism; Guanosine Triphosphate/metabolism; Hydrolysis; Molecular Sequence Data; Substrate Specificity; Sulfate Adenylyltransferase/genetics; Sulfate Adenylyltransferase/metabolism |
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