Information on EC 2.4.2.18 - anthranilate phosphoribosyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.4.2.18
-
RECOMMENDED NAME
GeneOntology No.
anthranilate phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tryptophan biosynthesis
-
-
tryptophan metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-alpha-D-ribosyltransferase
In some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan [EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
CAS REGISTRY NUMBER
COMMENTARY hide
9059-35-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
mutant ups1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild-type and 5-methyltryptophan resistant mutant
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Enterobacter liquefaciens
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-2-pentenoate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-amino-2-pentenoate + diphosphate
show the reaction diagram
-
good substrate
-
-
?
2-aminoacrylate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-aminoacrylate + diphosphate
show the reaction diagram
-
-
-
-
?
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-aminocrotonate + diphosphate
show the reaction diagram
-
good substrate
-
-
?
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-enamine + diphosphate
show the reaction diagram
-
-
reaction product predicted to be a phosphoribosyl-enamine adduct, which breaks down directly into phosphoribosyl amine and 2-ketobutyrate (a reaction mediated by TrpD or non-enzymatic), or which breaks down non-enzymatically into ribose 5'-phosphate, 2-ketobutyrate and NH3. Ribose 5'-phosphate and NH3 combine non-enzymatically to form phosphoribosyl amine
-
?
ammonia + 5-phospho-alpha-D-ribose 1-diphosphate
phosphoribosyl amine + diphosphate
show the reaction diagram
-
anthranilate synthase-phosphoribosyl transferase complex subunit TrpD in vitro
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
show the reaction diagram
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
additional information
?
-
-
connections between purine, thiamine, and tryptophan biosynthetic pathways, overview, the enzyme complex can substitute for PurF in formation of phosphoribosyl amine in vivo
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Hydroxyanthranilate
Hansenula henricii
-
competitive
5-Methyltryptophan
-
0.32 mM
anthranilate
L-tryptophan
Mg2+
-
marked inhibition at MgCl2 concentrations higher than 0.1 mM
N-(5-phospho-D-ribosyl)-anthranilate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme is upregulated during biotic and abiotic stress
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 1.54
5-phospho-alpha-D-ribose 1-diphosphate
0.000005 - 0.297
anthranilate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 6
5-phospho-alpha-D-ribose 1-diphosphate
0.035 - 13.3
anthranilate
additional information
5-phospho-alpha-D-ribose 1-diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84 - 76
5-phospho-alpha-D-ribose 1-diphosphate
158
0.56 - 540
anthranilate
474
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
3-Hydroxyanthranilate
Hansenula henricii
-
-
0.03
anthranilate
Hansenula henricii
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.7
Hansenula henricii
-
-
7.6
-
assay at, formation of N-(5-phospho-D-ribosyl)-anthranilate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32400
-
double mutant M47D/I36E, analytical-gel filtration chromatography
34100
-
double mutant M47D/I36E, analytical ultracentrifugation (sedimentation equilibrium)
38800
-
calculated for monomeric wild-type and mutants
60100
-
mutant M47D, analytical ultracentrifugation (sedimentation equilibrium)
61700
-
mutant M47D, analytical gel filtration chromatography
63400
-
mutant I36E, analytical gel filtration chromatography
64500
-
wild-type, analytical gel filtration chromatography
66000
-
mutant I36E, analytical ultracentrifugation (sedimentation equilibrium)
72200
-
wild-type, analytical ultracentrifugation (sedimentation equilibrium)
73300
-
gel filtration; gel filtration
77700
-
calculated for the dimeric wild-type and mutants
83000
-
sedimentation equilibrium
90000
-
tryptophan auxotroph with no anthranilate synthase activity, sucrose density gradient sedimentation
150000
-
and 70000, disc gel electrophoresis
170000
-
sucrose density gradient sedimentation, complex with anthranilate synthase activity
220000
-
and larger than 1000000, strain trpAB1653trpR782, gel filtration
320000
-
strain TAX6trpR782, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
monomer or dimer
-
equilibrium between minor, thermo-labile monomeric and major, thermo-stable dimeric state of single mutants M47D (dissociation constant, KD: 17 +/-10 microM) and I36E (KD: 0.8 +/-0.6 microM), analytical ultracentrifugation (sedimentation equilibrium)
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzymes N138A, P180A, R193L, R193A, R194A, and G107P, hanging drop vapor diffusion method, using
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hanging drop vapor diffusion method, complexed with Mn2+ diphosphate
-
crystal structures of the wild-type enzyme complexed to its two natural substrates anthranilate and 5-phosphoribosyl-1-pyrophosphate/Mg2+
-
hanging-drop method, crystals of ssTrpD diffract to better than 2.6 A resolution; hanging drop vapor diffusion method
-
mutant D83G/F149S in complex with 5-phospho-alpha-D-ribose 1-diphosphate and Mn2+, to 2.25 A resolution. Protein backbone of mutant D83G/F149S shows no detectable differences to the wild-type enzyme, whereas 5-phospho-alpha-D-ribose 1-diphosphate bound to mutant D83G/F149S adopts an extended conformation that contrasts markedly with the S compact shape observed in complexes of the wild-type enzyme
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mutant M47D, structurally very similar to wild-type (rms deviation of 0.7 A for most of equivalent C(alpha) atoms) but reduced buried surface area per subunit compared to wild-type homodimer, Aps47 protonated at pH 6, crystals of space group P2 with four molecules (two homodimers) per asymmetric unit and A2 pseudo-symmetry, unit cell parameters a=91.6 A, b=65.9 A, c=115.7 A, beta=107.4, 45% (v/v) solvent content, hanging drop method: 1 microlitre protein solution (5 mg/ml) + 1 microlitre reservior solution (50 mM MES pH 6.0, 18% (v/v) PEG, 5% (v/v) glycerol), room temperature, 72 h
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the crystal structure of the dimeric class III phosphoribosyltransferase. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is coordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
loss of 10% activity in 24 h
46
-
half-life: strain TAX6trpR782: 1.5 min, strain trpAB1653trpR782: 5 min
70
-
50% loss of activity after 69 min; t1/2: 69 min, addition of anthranilate has no stabilizing effect
80
-
half-lives (t1/2) as measure of kinetic stability, t1/2(wild-type): 40 min, t1/2(double mutant M47D/I36E): 3 min, t1/2(mutant I36E, about 1 microM): 3 min, t1/2(mutant I36E, about 20 microM): 40 min, t1/2(mutant M47D, about 1 microM): 4 min, t1/2(mutant M47D, about 47 microM): 15 min, irreversible heat inactivation (pH 6.7) at different time points followed by chilling, centrifugation and estimation of residual activity
82
-
double mutant I36E/M47D, 12 microM, melting temperature at which half of the protein is unfolded deduced from DSC, pH 7.5
83
-
mutant M47D, 12 microM, melting temperature at which half of the protein is unfolded deduced from DSC, pH 7.5
85
-
50% loss of activity after 35 min; t1/2: 35 min, addition of anthranilate has no stabilizing effect
92
-
wild-type, 12 microM, melting temperature at which half of the protein is unfolded deduced from differential scanning calorimetry (DSC), pH 7.5
additional information
-
concentration-dependent kinetic stability of single mutants I36E and M47D during heat inactivation at 80C; dimerisation stabilizes against thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution inactivates
-
freezing and thawing inactivates
-
glycerol, 10%, is essential for storage, but it must be replaced by polyethylene glycol to achieve crystals that are not severely temperature dependent and radiation sensitive
-
the enzyme is either digested by trypsin, V8-protease or thermolysin after incubation for 1 h at 25C but not by thermolysin at 70C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, crude extract is stable for 2 years
-
-25C, 500 mM Tris-HCl, pH 7.5, 2 mM EDTA, 2 mM MgCl2, 5% loss of activity after 2 weeks
Hansenula henricii
-
4C, 10% loss of activity after 2 months
-
addition of 10% glycerol at -70C and then dropping the solution into liquid N2, can be thawed and frozen several times without loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from Escherichia coli extract by heat-precipitation of host proteins followed by metal chelate affinity chromatography, yield of 0.4-0.8 mg protein per 1 g wet cell mass, >95% purity, stored at -80C
-
immobilized metal ion affinity chromatography (Ni2+)
-
Ni-NTA column chromatography
-
partial, enzyme complex
-
wild-type and mutants purified by heat precipitation and metal chelate affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
-
amplified fragments containing the full-length trpD gene ligated into the pQE40 vector, transformed into Escherichia coli competent DH5alpha cells. Wild-type and its mutants expressed heterologously in Escherichia coli strain W3110 trpEA2trpEA2, containing the helper plasmid pDM,1
-
expressed in Escherichia coli
-
His-tagged protein expressed in Escherichia coli
-
wild-type and mutants in pQE40 for expression with N-terminal hexa-His tag in Escherichia coli W3110 trpEA2 (pDM)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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))
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 (80C) with half-lives from 3 to 40 min, no suitable crystal formed
I36E/M47D
-
mutation leads to monomerization, apparent melting temperature is 11.5C lower than the wild-type value
I36E/M47D/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 21.4C 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 17.4C 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 20.6C 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 20.9C 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 20.5C 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 18.5C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 13.3C 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 11.4C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M
-
mutation leads to monomerization, apparent melting temperature is 9.1C 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 8.7C 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 (80C) 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 80C 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 9.5C lower than the wild-type value
-
I36E/M47D/D83G/F149S
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mutation leads to monomerization, apparent melting temperature is 21.4C 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
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I36E/M47D/D83G/F149S/I169T
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mutation leads to monomerization, apparent melting temperature is 20.6C 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
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I36E/M47D/D83G/N109S/F149S
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mutation leads to monomerization, apparent melting temperature is 20.5C 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
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I36E/M47D/T77I/D83G/F149S
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mutation leads to monomerization, apparent melting temperature is 13.3C 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
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additional information
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution with indole-3-glycerophosphate synthetase
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