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2.4.2.18: anthranilate phosphoribosyltransferase

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

Word Map on EC 2.4.2.18

Reaction

N-(5-phospho-D-ribosyl)-anthranilate
+
diphosphate
=
anthranilate
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

AnPRT, anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyl transferase, anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyltransferase, anthranilate PRT, anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase, anthranilate-PP-ribose-P phosphoribosyltransferase, More, Pat, phosphoribosyl-anthranilate pyrophosphorylase, phosphoribosylanthranilate pyrophosphorylase, phosphoribosylanthranilate transferase, phosphoribosyltransferase, anthranilate, PR transferase, PRT, sAnPRT, ssAnPRT, SSO0890, ssTrpD, strpD, Trp D, TrpD, TTC1491

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.18 anthranilate phosphoribosyltransferase

Engineering

Engineering on EC 2.4.2.18 - anthranilate phosphoribosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D223N
kcat is 5.5fold higher than wild-type value at 2 mM Mg2+
D83G
inhibition by Mg2+ only at very high concentrations, alters the binding mode of the substrate Mg2+-5-phospho-alpha-D-ribose 1-diphosphate
D83G/F149S
E224Q
kcat is 5fold higher than wild-type value at 2 mM Mg2+
F149S
is inhibited by MgCl2 to a similar extent as wild-type, facilitates product release by increasing the conformational flexibility of the enzyme
H107A
kcat is 1.2fold higher than wild-type value at 0.05 mM Mg2+
H107A/P178A
kcat is 2.1fold lower than wild-type value at 0.05 mM Mg2+
I36E
weakened intersubunit interaction and increased protein solubility by introduction of negative side chain, monomer-dimer equilibrium (dissociation constant, KD: 0.8 +/-0.6 microM), concentration-dependent kinetic stability during heat inactivation (80°C) with half-lives from 3 to 40 min, no suitable crystal formed
I36E/M47D
mutation leads to monomerization, apparent melting temperature is 11.5°C lower than the wild-type value
I36E/M47D/D83G/F149S
mutation leads to monomerization, apparent melting temperature is 21.4°C lower than the wild-type value. kcat/Km for anthranilate is 14.5fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 33fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/F193S
mutation leads to monomerization, apparent melting temperature is 17.4°C lower than the wild-type value. kcat/Km for anthranilate is 52fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 31.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/I169T
mutation leads to monomerization, apparent melting temperature is 20.6°C lower than the wild-type value. kcat/Km for anthranilate is 8.9fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 24.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/L320M
mutation leads to monomerization, apparent melting temperature is 20.9°C lower than the wild-type value. kcat/Km for anthranilate is 11fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 31.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/N109S/F149S
mutation leads to monomerization, apparent melting temperature is 20.5°C lower than the wild-type value. kcat/Km for anthranilate is 39fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/N109S/F149S/I169T/L320M/N324I
mutation leads to monomerization, apparent melting temperature is 18.5°C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S
mutation leads to monomerization, apparent melting temperature is 13.3°C lower than the wild-type value. kcat/Km for anthranilate is 13.3fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
I36E/M47D/T77I/D83G/F149S/F193S
mutation leads to monomerization, apparent melting temperature is 11.4°C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M
mutation leads to monomerization, apparent melting temperature is 9.1°C lower than the wild-type value. kcat/Km for anthranilate is 85.7fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 2.7fold lower than kcat/Km for wild-type enzyme
I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M
mutation leads to monomerization, apparent melting temperature is 8.7°C lower than the wild-type value. kcat/Km for anthranilate is 209fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is higher than kcat/Km for wild-type enzyme
K106Q
kcat is 2.3fold lower than wild-type value at 2 mM Mg2+
M47D
weakened intersubunit interaction and increased protein solubility by introduction of negative side chain, monomer-dimer equilibrium (dissociation constant, KD: 17 +/-10 microM), concentration-dependent kinetic stability during heat inactivation (80°C) with half-lives from 4 to 15 min, no structural perturbation
M47D/I36E
double mutant, monomeric, similar catalytic efficiencies as the wild-type for both substrates, first-order kinetics for time-dependent but not concentration-dependent heat inactivation at 80°C with half-live t1/2: 3 min, no suitable crystal formed
R164A
kcat is 6.8fold lower than wild-type value at 0.05 mM Mg2+
R164A/H154A
kcat is 5.8fold lower than wild-type value at 0.05 mM Mg2+
D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 9.5°C lower than the wild-type value
-
I36E/M47D/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 21.4°C lower than the wild-type value. kcat/Km for anthranilate is 14.5fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 33fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/D83G/F149S/I169T
-
mutation leads to monomerization, apparent melting temperature is 20.6°C lower than the wild-type value. kcat/Km for anthranilate is 8.9fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 24.3fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/D83G/N109S/F149S
-
mutation leads to monomerization, apparent melting temperature is 20.5°C lower than the wild-type value. kcat/Km for anthranilate is 39fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/T77I/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 13.3°C lower than the wild-type value. kcat/Km for anthranilate is 13.3fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
-
D282A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
G308L
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
H307A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
K306A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
N309A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
P362L
-
mutation in enzyme complex subunit TrpD, increased activity compared to the wild-type enzyme
R364A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
T279A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
additional information
-
mutant ups1, i.e. underinducer after pathogen and stress 1, shows reduced enzyme expression and is defective in regulation of tryptophan biosynthetic enzymes and in camalexin accumulation, reduced defense against pathogen infection or after treatment with acifluorfen, phenotype and genotype analysis, overview