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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

Reaction

ATP
+
D-ribose 5-phosphate
=
AMP
 +
5-phospho-alpha-D-ribose 1-diphosphate

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

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.6 Diphosphotransferases
                2.7.6.1 ribose-phosphate diphosphokinase

Engineering

Engineering on EC 2.7.6.1 - ribose-phosphate diphosphokinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D58H
the mutant exhibits nearly identical sensitivity to ADP and GDP as the wild-type protein and has a notably greater phosphate requirement for activation
L135I
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
N120S
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
D58H
-
the mutant exhibits nearly identical sensitivity to ADP and GDP as the wild-type protein and has a notably greater phosphate requirement for activation
-
L135I
-
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
-
N120S
-
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
-
E206A
-
KM-value for ATP is 2.5fold higher than wild-type value
K197A
-
maximal velocity is reduced more than 30000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged
M208A
-
KM-value for ATP is 1.2fold higher than wild-type value
N203A
-
KM-value for ATP is 5.6fold higher than wild-type value
P200A
-
KM-value for ATP is 1.5fold lower than wild-type value
P202A
-
KM-value for ATP is 1.5fold higher than wild-type value
R198A
-
KM-value for ATP is nearly identical to wild-type value
R199A
-
maximal velocity is reduced more than 24000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged
R201A
-
KM-value for ATP is 2.9fold higher than wild-type value
V204A
-
KM-value for ATP is nearly identical to wild-type value
V207A
-
KM-value for ATP is 1.2fold lower than wild-type value
Q165P
mimicks missense mutations identified in human neurological disorders such as Arts syndrome
R228W
mimicks missense mutations identified in human neurological disorders such as Arts syndrome
G9S
-
mutation originates from prs-2 allele variant which is related to thermosensitive growth, decreased activity in comparison to the wild-type
K194A
-
mutation in conserved lysine residue, results in protein variant unable to synthetize 5-phospho-alpha-D-ribose 1-diphosphate
E43D
naturally occuring mutation causes the Rosenberg-Chutorian syndrome, the disease locus CMTX5 is situated on the chromosome band Xq21.32-q24
S132A
the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview
V142L
the mutation is associated with uric acid overproduction without gout but with developmental delay, hypotonia, hearing loss, and recurrent respiratory infections in human. The mutation affects both allosteric sites that are involved in inhibition of the enzyme and the ATP-binding site
Y146M
the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview
A181D
-
the mutant shows reduced specific activity compared to the wild type enzyme
D224A
-
the mutant shows reduced specific activity compared to the wild type enzyme
E306K
-
the mutant shows reduced specific activity compared to the wild type enzyme
G209V
-
the mutant shows 45fold reduced specific activity compared to the wild type enzyme
G50D
-
the mutant shows reduced specific activity compared to the wild type enzyme
A181D
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
D224A
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
E306K
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
G209V
-
the mutant shows 45fold reduced specific activity compared to the wild type enzyme
-
G50D
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
additional information