2.7.6.1: ribose-phosphate diphosphokinase
This is an abbreviated version!
For detailed information about ribose-phosphate diphosphokinase, go to the full flat file.
Word Map on EC 2.7.6.1
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2.7.6.1
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purine
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erythrocyte
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superactivity
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pyrimidine
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x-linked
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phosphoribosyltransferase
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uric
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gout
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hypoxanthine
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hypoxanthine-guanine
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deafness
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charcot-marie-tooth
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sensorineural
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hemolysates
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diphosphorylated
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nonsyndromic
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hgprt
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hyperuricaemia
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lesch-nyhan
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phosphoribosyl-pyrophosphate
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feedback-resistant
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synthesis
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medicine
- 2.7.6.1
- purine
- erythrocyte
-
superactivity
- pyrimidine
-
x-linked
- phosphoribosyltransferase
-
uric
- gout
- hypoxanthine
-
hypoxanthine-guanine
- deafness
- charcot-marie-tooth
-
sensorineural
-
hemolysates
-
diphosphorylated
-
nonsyndromic
- hgprt
-
hyperuricaemia
- lesch-nyhan
-
phosphoribosyl-pyrophosphate
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feedback-resistant
- synthesis
- medicine
Reaction
Synonyms
5-phospho-alpha D-ribosyl 1-diphosphate synthase, 5-phosphoribose pyrophosphorylase, 5-phosphoribosyl-1-alpha-diphosphate synthase, 5-phosphoribosyl-1-pyrophosphate synthetase, 5-phosphoribosyl-alpha-1-pyrophosphate synthetase, AN6711.2, ATP: D-ribose-5-phosphate pyrophosphotransferase, ATP:D-ribose-5-phosphate pyrophosphotransferase, bsPRS, Pcal_1127, phosphoribosyl diphosphate synthase, phosphoribosyl pyrophosphate synthase 1 (PRS-1), phosphoribosyl pyrophosphate synthase enzyme, phosphoribosyl pyrophosphate synthetase, phosphoribosyl-1-pyrophosphate synthetase, phosphoribosyl-diphosphate synthetase, phosphoribosylpyrophosphate synthase, phosphoribosylpyrophosphate synthetase, phosphoribosylpyrophosphate synthetase 1, phosphoribosylpyrophosphate synthetase subunit 1, PP-ribose P synthetase, PPRibP synthetase, PRibPP synthase, PRPP synthase, PRPP synthetase, PRPPase, PRPPS, PRPPS1, PRPPS2, PRPS1, Prps1a, Prps1b, PRS, PRS-I, PRS1, Prs4, PrsA, PrsB, PrsC, pyrophosphokinase, ribose phosphate, pyrophosphoribosylphosphate synthetase, ribophosphate pyrophosphokinase, ribose-5-phosphate pyrophosphokinase, ribose-phosphate pyrophosphokinase, ribose-phosphate pyrophosphokinase 1, RPPK, SSO1045, TT_C1184, TT_C1274
ECTree
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General Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the phosphoribosyl diphosphate synthetase family, enzymes of this family are widespread in different eukaryotic and prokaryotic organisms and are involved in a number of important biochemical processes associated with purine and pyrimidine metabolism
malfunction
physiological function
malfunction
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the reduction of enzyme activity causes both premature and hyperseptation
malfunction
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the reduction of enzyme activity causes both premature and hyperseptation
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physiological function
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normal cytokinesis is dependent on a normal level of enzyme activity. The enzyme is required for the proper timing of septation
physiological function
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the enzyme is crucial for mycobacterial cell wall biosynthesis
physiological function
the increased expression level of ribose-phosphate pyrophosphokinase 1 plays roles in the regulation of deltamethrin resistance
physiological function
ribose-5-phosphate diphosphokinase catalyzes the transfer of pyrophosphoryl group from ATP to C1 hydroxyl group of ribose-5-phosphate resulting in the production of AMP and phosphoribosyl diphosphate, the latter plays a central role in several processes of life, including the synthesis of nucleotides, co-enzyme NAD+, and amino acids histidine and tryptophan
physiological function
the enzyme produces 5-phosphoribosyl diphosphate which is an essential metabolite and an allosteric regulator in the de novo and salvage pathways of the biosynthesis of purine and pyrimidine nucleotides, pyrimidine-containing enzyme cofactors, and the amino acids histidine and tryptophan. Due to the key role of the enzyme in cell metabolism, the activity of these enzymes is tightly regulated by an excess of the substrate via feedback inhibition, as well as by allosteric interactions through the binding of ADP or GDP molecules in a special site between the subunits of the enzyme
physiological function
deletion of PrsA has no detectable effect on cellular morphology compared to that of the parental wild-type strain and PrsA is not required during hyphal elongation
physiological function
genome contains three PRPP synthase-homologous genes (PrsA, PrsB and PrsC).PrsB and PrsC are auxotrophic genes. The mRNA levels of PrsA, prsB and PrsC are dynamic during germination, hyphal growth and sporulation and show abundant expression during the vigorous hyphal growth. Inhibiting the expression of PrsB or prsC produces more effects on the total PRPP synthetase activity than inhibiting PrsA. The constitutive overexpression of PrsA or PrsC can rescue the defective phenotype of the PrsB-absent strain
physiological function
isoform Prps1a mutants display defects in the eye, the neuromast hair cells, and in pigmentation. Isoforms Prps1a/Prps1B double mutants at 5 days post fertilization have dysmorphic craniofacial features and very small eyes. Beyond the reduction in iridophores seen in the Prps1a homozygous mutants, the double mutants also display a reduction of melanocytes in both the head and the eyes late the first day after fertilization. The double mutant shows a dramatic reduction in body size with the majority of fish having a life span shorter than 40 days. Double mutant fish diplay a reduced number of inner ear hair cells and abnormal motor neuron development
physiological function
isoform Prps1b mutants show no overt phenotype. Mutant fish survive to adulthood, have a normal life span, and are able to normally reproduce. Isoforms Prps1a/Prps1B double mutants at 5 days post fertilization have dysmorphic craniofacial features and very small eyes. Beyond the reduction in iridophores seen in the Prps1a homozygous mutants, the double mutants also display a reduction of melanocytes in both the head and the eyes late the first day after fertilization. The double mutant shows a dramatic reduction in body size with the majority of fish having a life span shorter than 40 days. Double mutant fish diplay a reduced number of inner ear hair cells and abnormal motor neuron development
physiological function
PRPS is a direct target of retinoblastoma RB/E2F transcription factor in Drosophila melanogaster
physiological function
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PRS4 interacts in vivo with anaphase promoting complex/cyclosome subunit 10 (APC10)
physiological function
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genome contains three PRPP synthase-homologous genes (PrsA, PrsB and PrsC).PrsB and PrsC are auxotrophic genes. The mRNA levels of PrsA, prsB and PrsC are dynamic during germination, hyphal growth and sporulation and show abundant expression during the vigorous hyphal growth. Inhibiting the expression of PrsB or prsC produces more effects on the total PRPP synthetase activity than inhibiting PrsA. The constitutive overexpression of PrsA or PrsC can rescue the defective phenotype of the PrsB-absent strain
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physiological function
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deletion of PrsA has no detectable effect on cellular morphology compared to that of the parental wild-type strain and PrsA is not required during hyphal elongation
-
physiological function
-
normal cytokinesis is dependent on a normal level of enzyme activity. The enzyme is required for the proper timing of septation
-
physiological function
-
ribose-5-phosphate diphosphokinase catalyzes the transfer of pyrophosphoryl group from ATP to C1 hydroxyl group of ribose-5-phosphate resulting in the production of AMP and phosphoribosyl diphosphate, the latter plays a central role in several processes of life, including the synthesis of nucleotides, co-enzyme NAD+, and amino acids histidine and tryptophan
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physiological function
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the enzyme is crucial for mycobacterial cell wall biosynthesis
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