Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase

In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].

9031-60-1

-

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

1-(3-indolyl)glycerol-3-phosphate + CO2 + H2O

2 entries

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O

15 entries

1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O

38 entries

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O

2 entries

1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

?

27 entries

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

indoleglycerol phosphate + CO2 + H2O

Saccharolobus solfataricus

-

724261

Substrates: -
Products: -

?

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate + ?

1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O

4 entries

1-(phenylamino)-1-deoxy-D-ribulose-5-phosphate

1-C-(indol-3-yl)glycerol 3-phosphate + H2O

2 entries

additional information

?

-

2 entries

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

1-(3-indolyl)glycerol-3-phosphate + CO2 + H2O

Mycobacterium tuberculosis

-

701916

Substrates: -
Products: -

?

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O

7 entries

1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O

Thermotoga maritima

-

652796

Substrates: -
Products: -

ir

1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

?

27 entries

Ca2+

Mycobacterium tuberculosis

-

significantly affects activity, the optimal concentration is about 0.4-2.0 mM

678351

Mg2+

Mycobacterium tuberculosis

-

significantly affects activity, the optimal concentration is about 0.4-2.0 mM

678351

Mn2+

Mycobacterium tuberculosis

-

significantly affects activity, the optimal concentration is about 0.4-2.0 mM

678351

Na+

Mycobacterium tuberculosis

-

significantly affects activity, the optimal concentration is about 0.4-2.0 mM

678351

ATB107

4 entries

geomycine

Mycobacterium tuberculosis

-

0.5 mg/ml

678351

H2O2

Mycobacterium tuberculosis

-

0.001% H2O2 inactivates the enzyme almost completely

678351

kanamycin

Mycobacterium tuberculosis

-

0.5 mg/ml

678351

L-tryptophan

Mycobacterium tuberculosis

P9WFX7

tryptophan at high concentrations has definite inhibitory activity against Mycobacterium tuberculosis but does not antagonize the activity of ATB107

692324

methanol

Mycobacterium tuberculosis

-

enzyme activity is gradually lost in the presence of increasing concentrations of methanol and completely lost at 65%

678351

phosphate

Thermotoga maritima

-

648890

reduced 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate

Pseudomonas aeruginosa

P20577

nonreactive substrate analogue, binds in the active site

772833

-

Reduced 1-[2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate

Escherichia coli

-

4611

-

streptomycin

Mycobacterium tuberculosis

-

0.5 mg/ml

678351

tryptophan

Mycobacterium tuberculosis H37Ra

A5U2W7

tryptophan at high concentrations has definite inhibitory activity against Mycobacterium tuberculosis but does not antagonize the activity of ATB107

692324

additional information

4 entries

-

0.000013 - 0.14

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

36 entries

0.000006 - 21.67

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

51 entries

0.18

1-(phenylamino)-1-deoxy-D-ribulose-5-phosphate

Pseudomonas aeruginosa

P20577

pH 7, 22°C

772833

-

0.001 - 11.1

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

38 entries

0.025 - 7.2

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

23 entries

0.0044

1-(phenylamino)-1-deoxy-D-ribulose-5-phosphate

Pseudomonas aeruginosa

P20577

pH 7, 22°C

772833

-

1.36 - 20000

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

36 entries

100 - 14200

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate

8 entries

0.024

1-(phenylamino)-1-deoxy-D-ribulose-5-phosphate

Pseudomonas aeruginosa

P20577

pH 7, 22°C

772833

-

0.27

phosphate

Thermotoga maritima

-

60°C

648890

0.004

Mycobacterium tuberculosis

-

recombinant enzyme, at 37°C, pH 7.0

1.8

-

15.2

55°C, pH 5.5

2.3

3.2

-

3.7

-

300

-

69

-

additional information

Escherichia coli

-

rapid and sensitive continous spectrophotofluorometric assay that can be used in presence of glycerol

4598

5.5

2 entries

7

Mycobacterium tuberculosis

-

in 5 mM Tris-HCl buffer

7 - 7.5

-

7.5

4.5 - 8

Mycobacterium tuberculosis

-

701916

5.5 - 8

Mycobacterium tuberculosis

-

in 5 mM Tris-HCl buffer

678351

7 - 8.2

Pseudomonas aeruginosa

-

activity begins to decrease above pH 8.2 and is 70% of maximum at pH 9.0

100

-

25

37

75

Saccharolobus solfataricus

Q06121

assay

725533

84

Saccharolobus solfataricus

-

4612

85

Thermococcus kodakarensis

Q9YGB5

-

723195

15 - 35

Mycobacterium tuberculosis

-

activation energy value of 8.4 kcal/mol, the linearity of the Arrhenius plot demonstrates that there is no change in the rate-limiting step in the temperature range employed

701916

60 - 95

Thermococcus kodakarensis

Q9YGB5

60°C: about 50% of maximal activity, 95°C: about 45% of maximal activity

723195

6.8

Pyrococcus furiosus

Q8U088

calculated from sequence

771013

Acinetobacter calcoaceticus

-

4605

-

Aeromonas caviae

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

-

-

-

-

-

Chromobacterium violaceum

-

4607

-

Citrobacter freundii

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Corynebacterium glutamicum

bifunctional N-(5-phosphoribosyl)anthranilate isomerase/indole-3-glycerolphosphate synthase, cf. EC 5.3.1.24

772491

P06560

UniProt

Corynebacterium glutamicum ATCC 13032

bifunctional N-(5-phosphoribosyl)anthranilate isomerase/indole-3-glycerolphosphate synthase, cf. EC 5.3.1.24

772491

P06560

UniProt

Enterobacter cloacae

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Enterobacter cloacae subsp. dissolvens

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Enterobacter liquefaciens

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Escherichia coli

2 entries

Escherichia coli W3110 / ATCC 27325

-

4598

-

Euglena gracilis

multifunctional enzyme with the activities of Ec 4.1.4.27, Ec 4.2.2.18, Ec 4.1.1.48 and Ec 4.2.1.20

4603

-

Hafnia alvei

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

-

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Mycobacterium tuberculosis

3 entries

Mycobacterium tuberculosis H37Ra

-

692324

A5U2W7

UniProt

Mycobacterium tuberculosis H37Rv

2 entries

Mycobacterium tuberculosis Rv3246c

-

715893

-

Mycobacterium tuberculosis variant bovis BCG

-

UniProt

-

-

Pectobacterium carotovorum

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4596, 4599

-

Proteus vulgaris

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4596, 4599

-

Pseudomonas aeruginosa

2 entries

Pseudomonas aeruginosa DSM 22644

-

UniProt

-

-

-

UniProt

Saccharolobus solfataricus

10 entries

Saccharolobus solfataricus DSM 1617

-

747469

Q06121

Uniprot

Saccharolobus solfataricus P2

-

721686, 725533

Q06121

Uniprot

Saccharomyces cerevisiae

2 entries

Salmonella enterica subsp. enterica serovar Typhimurium

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4596, 4606

-

Serratia marcescens

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4596, 4599, 4601

-

Serratia rubidaea

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24

4599

-

Staphylococcus aureus

wild-type strain 655 and mutant strains

4600

-

Thermococcus kodakarensis

-

SwissProt

-

UniProt

Thermus thermophilus HB8 / ATCC 27634 / DSM 579

-

UniProt

-

-

Vitis vinifera x Vitis riparia

-

706809

-

Vitis vinifera x Vitis vinifera

-

706809

-

Zea mays

2 entries

[Brevibacterium] flavum

possibly forms a bifunctional enzyme with phosphoribosylanthranilate isomerase, Ec4.1.1.48/Ec5.3.1.24

4595

-

culture condition:oleate-grown cell

isoforms IGPS1, 2, and 3

9507

775111

Highest Expressing Human Cell Lines

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Cell Line Links

Gene Links

evolution

Zea mays

B4G1Z5

the maize genome encodes indole-3-glycerolphosphate synthase isoforms IGPS1, 2, and 3. IGPS2 is similar to enzymes found in both monocots and dicots, whereas maize IGPS1 and IGPS3 are in monocot-specific clades

775111

metabolism

3 entries

physiological function

Brucella abortus 2308

Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819

2 entries

Corynebacterium glutamicum ATCC 13032

2 entries

Escherichia coli

5 entries

Mycobacterium tuberculosis

Mycobacterium tuberculosis H37Rv

Pseudomonas aeruginosa

11 entries

Saccharolobus solfataricus

4 entries

Saccharolobus solfataricus P2

155000

-

2 * 155000, SDS-PAGE

4603

21000

Saccharolobus solfataricus

-

gel filtration

4612

22000

Chromobacterium violaceum

-

gel filtration

4607

23500

2 entries

23600

Thermotoga maritima

-

gel filtration

648890

24200

Thermotoga maritima

Q56319

gel filtration, N-terminal deletion mutant lacking 25 amino acids

25000

gel filtration

26300

Saccharolobus solfataricus

Q06121

gel filtration, wild-type

664084

26400

Saccharolobus solfataricus

Q06121

1 * 26400, N-terminal deletion mutant lacking 26 amino acids, 1 * 28600, wild-type, calculated

664084

26600

2 entries

27000

Saccharolobus solfataricus

-

1 * 27000, SDS-PAGE

4612

28000

Mycobacterium tuberculosis

-

SDS-PAGE, recombinant enzyme

678351

28200

Thermotoga maritima

Q56319

gel filtration, wild-type

664084

28566

Saccharolobus solfataricus

-

1 * 28566, calculation from nucleotide sequence

4612

28600

2 entries

28700

3 entries

30000

Mycobacterium tuberculosis

-

gel-filtration chromatography

701916

31000

3 entries

32000

Pseudomonas putida

-

gel filtration

4608

320000 - 340000

Neurospora crassa

-

anthranilate synthetase complex, gel filtration

4604

325000

Euglena gracilis

-

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, gel filtration

4603

39300

Thermotoga maritima

Q56319

gel filtration, N-terminal deletion mutant lacking 25 amino acids

664084

44000

Klebsiella aerogenes

-

equilibrium sedimentation

45000

47000

47100

gel filtration, wild-type

48000

53000

70000

-

2 * 94000 + 2 * 70000, anthranilate synthetase complex, one subunit is a trifunctional peptide which contains the catalytic sites for the phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase reactions, and associates with the second subunit to form glutamine-dependent anthranilate synthetase, SDS-PAGE

4604

94000

Neurospora crassa

-

2 * 94000 + 2 * 70000, anthranilate synthetase complex, one subunit is a trifunctional peptide which contains the catalytic sites for the phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase reactions, and associates with the second subunit to form glutamine-dependent anthranilate synthetase, SDS-PAGE

?

dimer

monomer

tetramer

-

2 * 94000 + 2 * 70000, anthranilate synthetase complex, one subunit is a trifunctional peptide which contains the catalytic sites for the phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase reactions, and associates with the second subunit to form glutamine-dependent anthranilate synthetase, SDS-PAGE

4604

additional information

4 entries

additional information

Saccharolobus solfataricus

-

kinetic studies of folding mechanism

652889

crystal structure of apo enzyme and in complex with substrate analogue reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate, to 2.1 A and 2.2 A resoultion, respectively. TrpCF shows a conformational change at the loops upon substrate binding

Corynebacterium glutamicum

-

-

structure in complex with nonreactive substrate analogue, reduced 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate. There are eight molecules in the asymmetric unit, of which seven contain ligand and one displays a conformation closer to the reactive state

Pseudomonas aeruginosa

P20577

772833

2.0 A structure

Saccharolobus solfataricus

Q06121

4615

crystal packing seems to be influenced by ionic strength of the solvent

Saccharolobus solfataricus

-

4613

in complex with substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, with a substrate analogue, and with product indole-3-glycerol phosphate

Saccharolobus solfataricus

Q06121

652887

molecular dynamics simulations of wild-type at 25°C in the apo form and in the presence of the substrate

Saccharolobus solfataricus

Q06121

747143

mutagenesis data and crystal structure analysis of IGPS from Sulfolobus solfataricus allows for the formulation of a plausible chemical mechanism of the reaction

Saccharolobus solfataricus

Q06121

721686

N-terminal deletion mutant lacking 26 amino acids, structure of core is unchanged compared to wild-type

Saccharolobus solfataricus

Q06121

664084

vapour diffusion method in hanging drops, the 2.0 A crystal structure is determined and compared with the known 2.0 A structure of the IGPS domain of the bifunctional enzyme from Escherichia coli. Both enzymes have only 30% sequence identity, but share high structural similarity

Saccharolobus solfataricus

Q06121

4615

contains 17 strong salt bridges

-

-

I199T

Corynebacterium glutamicum

P06560

mutation in synthase domain, about 25% of wild-type catalytic activity

772491

I199V

Corynebacterium glutamicum

P06560

mutation in synthase domain, about 80% of wild-type catalytic activity

772491

L67K

Corynebacterium glutamicum

P06560

mutation in synthase domain, about 90% of wild-type catalytic activity

772491

V9I

Corynebacterium glutamicum

P06560

mutation in synthase domain, no change in catalytic activity

772491

I199T

Corynebacterium glutamicum ATCC 13032

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum ATCC 13032

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum ATCC 13032

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum ATCC 13032

-

mutation in synthase domain, no change in catalytic activity

-

I199T

Corynebacterium glutamicum BCRC 11384

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum BCRC 11384

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum BCRC 11384

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum BCRC 11384

-

mutation in synthase domain, no change in catalytic activity

-

I199T

Corynebacterium glutamicum DSM 20300

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum DSM 20300

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum DSM 20300

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum DSM 20300

-

mutation in synthase domain, no change in catalytic activity

-

I199T

Corynebacterium glutamicum JCM 1318

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum JCM 1318

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum JCM 1318

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum JCM 1318

-

mutation in synthase domain, no change in catalytic activity

-

I199T

Corynebacterium glutamicum LMG 3730

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum LMG 3730

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum LMG 3730

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum LMG 3730

-

mutation in synthase domain, no change in catalytic activity

-

I199T

Corynebacterium glutamicum NCIMB 10025

-

mutation in synthase domain, about 25% of wild-type catalytic activity

-

I199V

Corynebacterium glutamicum NCIMB 10025

-

mutation in synthase domain, about 80% of wild-type catalytic activity

-

L67K

Corynebacterium glutamicum NCIMB 10025

-

mutation in synthase domain, about 90% of wild-type catalytic activity

-

V9I

Corynebacterium glutamicum NCIMB 10025

-

mutation in synthase domain, no change in catalytic activity

-

L55S

Escherichia coli

-

Lys55Ser with 60fold decrease in turnover-number and 450fold increase in Km-value

4614

L5V

Escherichia coli

-

Leu5Val without effect on turnover-number and Km

4609

E168A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

H170A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

L193A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

L196A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

N189A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

N192A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

P63A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

R191A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

S64A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

V169A

Mycobacterium tuberculosis

P9WFX7

site directed mutagenesis

692324

E168A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

H170A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

L193A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

L196A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

N189A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

N192A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

P63A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

R191A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

S64A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

V169A

Mycobacterium tuberculosis H37Ra

A5U2W7

site directed mutagenesis

692324

E168A

Mycobacterium tuberculosis H37Rv

-

site directed mutagenesis

-

P63A

Mycobacterium tuberculosis H37Rv

-

site directed mutagenesis

-

S64A

Mycobacterium tuberculosis H37Rv

-

site directed mutagenesis

-

V169A

Mycobacterium tuberculosis H37Rv

-

site directed mutagenesis

-

Phe201

2 entries

D61C

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value

721686

E210Q

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 6fold lower than wild-type value

725533

E51Q

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 28fold lower than wild-type value

725533

F246S

2 entries

F89A

Saccharolobus solfataricus

-

approximately 24fold increase in the KM-value, eleven-fold decrease in the maximum turnover rate

726453

G212E

2 entries

K53Q

Saccharolobus solfataricus

Q06121

low activity, kcat is 570fold lower than wild-type value

725533

K53R

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 500fold lower than wild-type value

725533

L236Q

Saccharolobus solfataricus

Q06121

mutation destabilizes helix alpha8'

747143

M237T

2 entries

N90A

Saccharolobus solfataricus

-

loss of the descending limb in the pH rate profile, 5-fold decrease in kcat at 25°C, but at higher temperatures (i.e. 75°C), the kinetic parameters for the N90A mutant enzyme closer to wild-type enzyme. Mutant enzyme has substantially reduced solvent deuterium kinetic isotope effects compared to wild-type enzyme at 75°C. 2fold decrease in the rate of thermal inactivation at 90°C as compared to wild-type enzyme

726453

N90Q

Saccharolobus solfataricus

-

the steady-state kinetics for the mutant enzyme are substantially decreased compared to wild-type enzyme at lower temperatures, but kcat of the N90Q variant approaches that of wild-type enzyme at higher temperatures. The solvent deuterium kinetic isotope effects on kcat is also substantially reduced compared to wild-type enzyme. 2fold decrease in the rate of thermal inactivation at 90°C

726453

P2S

Saccharolobus solfataricus

-

slight increase in kcat/Km (substrate: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate). Mutant enzyme is about as thermostable as wild-type enzyme

724261

P2S/F246S

Saccharolobus solfataricus

-

about 2fold increase in turnover-number, 8fold increase in KM-value, decrease in kcat/Km

724261

P2S/G212E

Saccharolobus solfataricus

-

about 4fold increase in turnover-number,200fold increase in Km-valuer, decrease in kcat/Km

724261

R182A

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 39fold lower than wild-type value

725533

R18C

Saccharolobus solfataricus

Q06121

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value

721686

R54A

Saccharolobus solfataricus

-

mutation does not result in any substantial change to the steady-state kinetic parameters at any of the temperatures assayed (25°C, 37°C, 75°C). At 75°C, the mutant enzyme shows a small increase to kcat (about 1.8 fold) compared to wild-type enzyme. Mutant enzyme has substantially reduced solvent deuterium kinetic isotope effects compared to wild-type enzyme at 75°C. Thermal inactivation constant at 90°C is similar to wild-typ enzyme

726453

R54A/N90A

Saccharolobus solfataricus

-

the R54A/N90A double substitution are not additive with the effects of the R54A and N90A single substitutions suggesting some type of thermodynamic coupling between these residues

726453

R64A/D65A

Saccharolobus solfataricus

Q06121

mutation disrupts interactions on the C-terminal side of the beta1alpha1 loop and decreases catalytic efficiency, slows down the dehydration step and quenches loop dynamics

747469

R64A/D65A/N90A

Saccharolobus solfataricus

Q06121

mutation leads to new micros-ms timescale loop dynamics and makes the ring-closure step rate-determining once again

747469

R64A/D65A

Saccharolobus solfataricus DSM 1617

-

mutation disrupts interactions on the C-terminal side of the beta1alpha1 loop and decreases catalytic efficiency, slows down the dehydration step and quenches loop dynamics

-

R64A/D65A/N90A

Saccharolobus solfataricus DSM 1617

-

mutation leads to new micros-ms timescale loop dynamics and makes the ring-closure step rate-determining once again

-

D61C

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value

-

E210Q

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 6fold lower than wild-type value

-

E51Q

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 28fold lower than wild-type value

-

K53Q

Saccharolobus solfataricus P2

-

low activity, kcat is 570fold lower than wild-type value

-

K53R

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 500fold lower than wild-type value

-

R182A

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 39fold lower than wild-type value

-

R18C

Saccharolobus solfataricus P2

-

kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value

-

D184A

Thermotoga maritima

-

no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability

652796

R241A

Thermotoga maritima

-

no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability

652796

additional information

11 entries

5

Mycobacterium tuberculosis

-

slight activity at pH 5.0

678351

8

Mycobacterium tuberculosis

-

almost no activity at pH 8.0

678351

additional information

Saccharolobus solfataricus

-

melting temperature is higher at alkaline that at neutral pH

100

half-life 200 min

40 - 50

Mycobacterium tuberculosis

-

little loss of activity after a 10 min heating in a water bath at temperatures from 40 to 50°C

678351

44

Escherichia coli

-

half-life: 1.8 min

4615

73

Thermotoga maritima

-

335 min, half-life for irreversible thermal inactivation

75

80

83.5

-

110 min, half-life for irreversible thermal inactivation

652796

84

Thermotoga maritima

-

110 min, half-life for irreversible thermal denaturation

648890

85.5

3 entries

86.5

Saccharolobus solfataricus

-

in 0.05 M potassium phosphate at pH 7.5. Half-life of wild-type enzyme: 46 min, half-life of mutant enzyme P2S: 18 min, hal-life of mutant enzyme F246S 1 min, half-life of mutant enzyme G212E: 38 min, half-life of mutant enzyme P2S/F246S: less than 0.1 min, half-life of mutant enzyme P2S/G212E: 19 min

724261

89

Saccharolobus solfataricus

Q06121

half-life: 4.4 min

4615

90

2 entries

additional information

4 entries

guanidinium-induced denaturation. Unfolding mechanism closely approaches a two-state model at pH 7.0 and a more complex mechanism at pH 9.0

Saccharolobus solfataricus

-

4610

half-life after trypsinolysis in 0.1 M Tris acetate at pH 7.8 and 25°C: wild-type enzyme (120 min), mutant enzyme P2S (60 min), mutant enzyme F246S (40 min), mutant enzyme G212E (40 min), mutant enzyme P2S/F246S (8 min), mutant enzyme P2S/G212E (15 min)

Saccharolobus solfataricus

-

724261

optimal stabilization by 0.8 M sucrose

Bacillus subtilis

-

4593

the enzyme is strongly stabilized in phosphate buffer (t1/2: 46 min at 87°C) in comparison to HEPPS buffer (t1/2: 4.4 min at 89°C)

Saccharolobus solfataricus

-

724261

the higher stability of the enzyme from Sulfolobus solfataricus compared with the enzyme from E. coli seems to be the result of several improved interactions. Including a large number of salt bridges, stabilization of alpha-helices and strengthening of both polypeptide chain termini and solvent-exposed loops

2 entries

urea

Saccharolobus solfataricus

Q06121

the structure of partially folded states of the enzyme is assessed by hydrogen exchange mass spectrometry and Gö model simulations. HX-MS analysis of the peptic peptides derived from the pulse-labeled product of the submillisecond folding reaction from the urea-denatured state reveal strong protection in the (betaalpha)4 region, modest protection in the neighboring (betaalpha)13 and (betaalpha)5beta6 segments and no significant protection in the remaining N and C-terminal segments. The results demonstrate that this species is not a collapsed form of the unfolded state under native-favoring conditions nor is it the native state formed via fast-track folding

681463

-70°C, 5 mM Tris-HCl (pH 7.0), at least 2 months, remains stable

Mycobacterium tuberculosis

-

678351

4°C, 1 mM potassium phosphate buffer pH 7.5, 1 mM dithiothreitol, stable for hours

Thermotoga maritima

-

648890

4°C, in presence of 0.8 M sucrose, 20% loss of activity

Bacillus subtilis

-

4593

-

10 entries

bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase

2 entries

chromatographic purification, Phenyl Sepharose High Sub FF column, ultrafiltration membrane (molecular weight cutoff) of 10,000 Da, Sephacryl S-100 column

Mycobacterium tuberculosis

-

701916

final step with Superdex-75 gel filtration

Saccharolobus solfataricus

-

681434

monofunctional enzyme

Escherichia coli

-

4611

multifunctional enzyme with the activities of Ec 4.1.4.27, Ec 4.2.2.18, Ec 4.1.1.48 and Ec 4.2.1.20

Euglena gracilis

-

4603

Ni-NTA His-binding resin affinity chromatography

Mycobacterium tuberculosis

-

678351

Q-Sepharose column chromatography

Escherichia coli

-

726866

TALON metal affinity resin column chromatography

Pseudomonas aeruginosa

-

728750

-

5 entries

expressed in Escherichia coli strain BL21

2 entries

expressed in Escherichia coli strain BL21 (DE3)

Mycobacterium tuberculosis

-

678351

expressed in Escherichia coli strain KK-8(pDM)

Pseudomonas aeruginosa

-

728750

expression in Escheichia coli

Pyrococcus furiosus

Q8U088

771013

expression in Escherichia coli

2 entries

expression in Escherichia coli BL21(DE3) STAR

Mycobacterium tuberculosis

-

701916

a significant increase in trp mRNA level is observed in cells grown in medium depleted of L-tryptophan, compared to cells grown in medium supplemented with L-tryptophan, indicating that expression of the gene cluster is regulated at the transcriptional level

Thermococcus kodakarensis

Q9YGB5

723195

ATB107 does not affect the expression of IGPS

2 entries

expression of isoform IGPS2 is not induced by insect feeding

Zea mays

B4G1Z5

775111

expression of isoforms IGPS1 and IGPS3 is induced by insect feeding

Zea mays

B4G1Z5

775111

initiated by rapid 11fold dilution in refolding buffer (10 mM phosphate pH 7.8 and 25°C)

Saccharolobus solfataricus

Q06121

681463

drug development

Mycobacterium tuberculosis

-

indole-3-glycerol phosphate synthase of Mycobacterium tuberculosis is an attractive target for new anti-Tuberculosis drug development

701916

medicine

4 entries

ExplorEnz (official portal for IUBMB Enzyme Nomenclature)

Expasy Enzyme Nomenclature Database

KEGG

SABIO-RK

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

Enzyme Nomenclature (alternative site)

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)