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Ligand 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.3.2.10

5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate

747052, 747861, 747057, 748120, 748148, 749381, 747285, 749228

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In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.3.1.16

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

0

-

Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.3.2.10

5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate

747057, 749228, 748120, 747861, 748148, 749381, 747052, 747285, 747058, 748246

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4.3.2.10

5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH3 = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O

749186

-

4.3.2.10

5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+ = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O

747057, 747058, 747285, 748148, 747052, 749228

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4.3.2.10

3 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.3.1.16

1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (22 results)

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Show Turnover Number (22 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.3.2.10

-999

-

pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes

747285

4.3.2.10

0.045

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A

747058

4.3.2.10

0.126

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R

747058

4.3.2.10

0.15

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A

747058

4.3.2.10

0.21

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H

747058

4.3.2.10

0.24

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A

747058

4.3.2.10

0.29

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R

747058

4.3.2.10

0.3

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K

747058

4.3.2.10

0.31

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R

747058

4.3.2.10

0.7

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A

747058

4.3.2.10

0.8

-

pH 8.0, 25°C, wild-type HisH-HisF complex

748148

4.3.2.10

0.845

-

30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme

747058

4.3.2.10

2.2

-

pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type

748148

4.3.2.10

3.9

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H

747058

4.3.2.10

3.9

-

pH 7.0, 30°C

749228

4.3.2.10

4.3

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A

747058

4.3.2.10

5

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R

747058

4.3.2.10

5.4

-

30°C, pH 7.0, cosubstrate: L-glutamine, wild-type enzyme

747058

4.3.2.10

5.4

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A

747058

4.3.2.10

6.1

-

pH 8.0, 30°C, cosubstrate: NH4+

747052

4.3.2.10

8.5

-

pH 8.0, 30°C, cosubstrate: L-glutamine

747052

4.3.2.10

8.7

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K

747058

4.3.2.10

22 entries

K_M Value (22 results)

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Show KM Value (22 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.3.2.10

-999

-

pH 7.0, 25°C, kinetic constants are determined for wild-type and mutant enzymes

747285

4.3.2.10

0.0015

-

pH 8.0, 25°C, wild-type HisH-HisF complex

748148

4.3.2.10

0.0015

-

pH 8.0, 30°C, cosubstrate: L-glutamine

747052

4.3.2.10

0.0016

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239K

747058

4.3.2.10

0.0017

-

pH 8.5, 25°C, ammonia-dependent reaction of isolated HisF subunit, wild-type

748148

4.3.2.10

0.0018

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360A

747058

4.3.2.10

0.002

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258R

747058

4.3.2.10

0.0023

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K360R

747058

4.3.2.10

0.003

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239A

747058

4.3.2.10

0.004

-

pH 7.0, 30°C

749228

4.3.2.10

0.005

-

30°C, pH 7.0, cosubstrate: L-glutamine, wild-type enzyme

747058

4.3.2.10

0.0079

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme R239H

747058

4.3.2.10

0.023

-

pH 8.0, 30°C, cosubstrate: NH4+

747052

4.3.2.10

0.046

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258R

747058

4.3.2.10

0.053

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239A

747058

4.3.2.10

0.055

-

30°C, pH 7.0, cosubstrate: NH4+, wild-type enzyme

747058

4.3.2.10

0.065

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360A

747058

4.3.2.10

0.072

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K360R

747058

4.3.2.10

0.075

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239H

747058

4.3.2.10

0.08

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme R239K

747058

4.3.2.10

0.098

-

30°C, pH 7.0, cosubstrate: L-glutamine, mutant enzyme K258A

747058

4.3.2.10

0.139

-

30°C, pH 7.0, cosubstrate: NH4+, mutant enzyme K258A

747058

4.3.2.10

22 entries

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

747052

8494895

Imidazole glycerol phosphate synthase the glutamine amidotransferase in histidine biosynthesis

1993

Klem, T.J.; Davisson, V.J.

Biochemistry

32

5177-5186

747057

12795595

Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase crystal structures of a ternary complex and the free enzyme

2003

Chaudhuri, B.N.; Lange, S.C.; Myers, R.S.; Davisson, V.J.; Smith, J.L.

Biochemistry

42

7003-7012

747058

12795596

Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase

2003

Myers, R.S.; Jensen, J.R.; Deras, I.L.; Smith, J.L.; Davisson, V.J.

Biochemistry

42

7013-7022

747285

15849257

Structural elements in IGP synthase exclude water to optimize ammonia transfer

2005

Amaro, R.E.; Myers, R.S.; Davisson, V.J.; Luthey-Schulten, Z.A.

Biophys. J.

89

475-487

747861

29468164

Glutamine hydrolysis by imidazole glycerol phosphate synthase displays temperature dependent allosteric activation

2018

Lisi, G.; Currier, A.; Loria, J.

Front. Mol. Biosci.

5

4

748120

12417026

Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8 open-closed conformational change and ammonia tunneling

2002

Omi, R.; Mizuguchi, H.; Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.

J. Biochem.

132

759-765

748148

11264293

Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex

2001

Beismann-Driemeyer, S.; Sterner, R.

J. Biol. Chem.

276

20387-20396

748246

19565337

Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima

2009

Lipchock, J.; Loria, J.P.

J. Biomol. NMR

45

73-84

749186

28396388

Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity

2017

Lisi, G.P.; East, K.W.; Batista, V.S.; Loria, J.P.

Proc. Natl. Acad. Sci. USA

114

E3414-E3423

749228

10733892

Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae

2000

Chittur, S.V.; Chen, Y.; Davisson, V.J.

Protein Expr. Purif.

18

366-377

749381

11839304

Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex

2002

Douangamath, A.; Walker, M.; Beismann-Driemeyer, S.; Vega-Fernandez, M.C.; Sterner, R.; Wilmanns, M.

Structure

10

185-193

Links to other databases for 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

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Show Links (1 entry)

ChEBI

PubChem

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