Adenosine phosphosulfate kinase

ADP NADH Disappearance Pyruvate Kinase, Lactate Dehydrogenase, and 3 -Nucleo-tidase Adenosine-5 -phosphosulfate Kinase ... 

Renosto, F., Seubert, P. A., and Segel, 1. H. (1984). Adenosine 5 -phosphosulfate kinase from Penicillium chrysogenum. Purification and kinetic characterization. J. Biol. Chem. 259, 2113-2123. 

H. Li, A. Deyrup, J. R. Mensch, Jr., M. Domowicz, A. K. Konstantinidis, N. B. Schwartz, The isolation and characterization of cDNA encoding the mouse bifunctional ATP sulfurylase-adenosine 5 -phosphosulfate kinase. J. Biol Chem. 1995 270, 29453-9. 

Kanno, N., Sato, M., and Sato, Y. (1990b) Purification and properties of adenosine-5 -phosphosulfate kinase from the marine red alga Porphyra yezoensis Ueda. Bot. Mar., 33, 369-374. 

Kinases and sulfotransferases utilize similar substrates and catalyze similar reactions. Both transfer anionic groups (Scheme 14.9). Both enzyme classes are capable of binding adenosine-based substrates. Sulfotransferases bind 3 -phospho-adenosine-5 -phosphosulfate (PAPS) (35) as a sulfate donor and kinases bind adenosine-5 -triphosphate (ATP) (36) as a phosphoryl donor. 

In a first step ATP and sulfate react to form adenosine-5 -phospho-sulfate (APS), a sulfate analog of ADP, and inorganic pyrophosphate. This reversible reaction is pulled by inorganic pyrophosphatase. The sulfurylase is not specific for sulfate, but also reacts with several other anions. In a second step, APS is phosphorylated in the 3 position in an irreversible kinase reaction in which ATP is the phosphate donor. The products of the kinase reaction are ADP and 3 -phosphoadenosine-5 -phosphosulfate (PAPS). ... 

The proteins NodP (ATP sulfurylase) and NodQ (adenosine 5 -phosphosulfate (APS) kinase) are associated in a sulfate-activating complex that enables the synthesis of the sulfate donor (PAPS) for Nod factor sulfation [42]. PAPS is also the sulfate donor used for the synthesis of cysteine and it is produced in E. coli by the normal household proteins CysC, CysD, and CysN [43, 44]. The genes cysCDN are part of the cysteine regulon which is repressed in the presence of cysteine and other reduced sulfur compounds [45]. This means that the E. coli machinery of PAPS biosynthesis can be used for chitin oligosaccharide sulfation if the bacteria are cultivated with sulfate as the only sulfur source. The total PAPS demand for the synthesis of cysteine and methionine (87 and 146 pmol g dried cells, respectively) [46] largely exceeds the maximum demand that can be estimated for chitin oligosaccharide sulfation (around 20 pmol g dried cells). 

Sulfotransferases catalyze the transfer of a sulfate (i.e., sulfonate, SO3) group from an activated donor onto the hydroxyl or less commonly the amino group of the acceptor molecule. The activated donor is invariably 3 phosphoadenosine 5 phosphosulfate (PAPS) [4]. PAPS is synthesized from ATP and S04 by the sequential action of ATP sulfurylase, which generates adenosine 5 phosphosulfate (APS), and APS kinase, which transfers a phosphate from ATP to APS. Chlorate, a drug which has been extremely useful for implicating the importance of sulfation... 

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