Enzyme - EC 2.7.6.1 - Ribose-phosphate pyrophosphokinase

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EC
 
2.7.6.1
Official Name
 
Ribose-phosphate pyrophosphokinase
Alternative Name(s)
 
Ribose-phosphate diphosphokinase
Phosphoribosyl pyrophosphate synthetase
Phosphoribosyl diphosphate synthetase
Class
 
2.Transferases
7.Transferring phosphorus-containing groups
6.Diphosphotransferases
Catalysed reaction
 
ATP + D-ribose 5-P AMP + 5-P-a-D-ribose-1-di-P
Substrates
 
ATP
dATP
D-Ribose 5-P
Products
 
AMP
dAMP
5-P-a-D-ribose-1-di-P
Metabolic Pathways
 
Other comments
 

dATP can also act as donor.

Phosphoribosyl pyrophosphate synthetase catalyzes the formation of PRPP from ATP and ribose 5-phosphate. PRPP is then used in various biosynthetic pathways, as for example in the formation of purines, pyrimidines, histidine and tryptophan. PRPP synthetase requires inorganic phosphate and magnesium ions for its stability and activity.

In mammals, three isozymes of PRPP synthetase are found; in yeast there are at least four isozymes.

As a signature pattern for this enzyme, it has been selected a very conserved region that has been suggested to be involved in binding divalent cations. This region contains two conserved aspartic acid residues as well as a histidine, which are all potential ligands for a cation such as magnesium.
Reference


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