Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.4.2.17: ATP phosphoribosyltransferase

This is an abbreviated version!
For detailed information about ATP phosphoribosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.17

Reaction

1-(5-phospho-beta-D-ribosyl)-ATP
+
diphosphate
=
ATP
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase, adenosine 5'-triphosphate phosphoribosyltransferase, adenosine triphosphate phosphoribosyltransferase, adenosine-triphosphate phosphoribosyltransferase, ATP phosphoribosyl transferase, ATP phosphoribosyl transferase complex, ATP phosphoribosyltransferase, ATP-phosphoribosyl transferase, ATP-phosphoribosyltransferase, ATP-PRT, ATP-PRT1, ATP-PRT2, ATP-PRTase, ATPPRT, HisG, HisGL, N-1-(5'-phosphoribosyl)-ATP transferase, phosphoribosyl ATP synthetase, phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase, phosphoribosyl-ATP pyrophosphorylase, phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase, phosphoribosyladenosine triphosphate pyrophosphorylase, phosphoribosyladenosine triphosphate synthetase, phosphoribosyltransferase, adenosine triphosphate

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.17 ATP phosphoribosyltransferase

Engineering

Engineering on EC 2.4.2.17 - ATP phosphoribosyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R216A
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
R216Q
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
R216A
-
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
-
R216Q
-
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
-
A249T
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
A270P
conserved residue
D213N
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
G230S
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
L231F/T235A
conserved residues
N215K
conserved residue
N215K/L231F/T235A
conserved residues, 37fold increase in Ki-value of histidine
N215K/L231F/T235A/A270P
conserved residues
S143F
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y
the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y/A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T228P
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T235M
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
D213N
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
G230S
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
S143F
-
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
T235M
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
D155A
-
slight increase in kcat, 3.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.7fold increase in Km-value for ATP
E130A
-
site-directed mutagenesis, about 60% reduced activity compared to the wild-type enzyme, no inhibition by histidine
K50A
-
2.3fold increase in kcat, 51fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.8fold increase in Km-value for ATP
K8A
-
2.5fold decrease in kcat, 4.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 3.1fold increase in Km-value for ATP
S140A
-
mutant is unstable, kinetic parameters can not be determined
T159A
-
2.2fold decrease in kcat, 280fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.5fold decrease in Km-value for ATP
T162A
-
3.2fold decrease in kcat, 49fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.6fold decrease in Km-value for ATP
Y268F/Y269F
-
site-directed mutagenesis, about 30% reduced activity compared to the wild-type enzyme, no inhibition by histidine
additional information