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Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase and Organism(s) Thermotoga maritima and UniProt Accession Q56320
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5.3.1.24 phosphoribosylanthranilate isomeraseIUBMB Comments
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 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
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Word Map
- 5.3.1.24
-
indoleglycerol
-
amidotransferase
-
alpha8
-
betaalpha8-barrels
-
dual-substrate
- biotechnology
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
prai, phosphoribosyl anthranilate isomerase, phosphoribosylanthranilate isomerase, n-(5'-phosphoribosyl)anthranilate isomerase, pra isomerase, ttprai, trpfctl2, phosphoribosyl isomerase a, trp1p, pftrpf, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
-
-
-
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isomerase, phosphoribosylanthranilate
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-
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N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
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N-5-phosphoribosylanthranilate isomerase
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-
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PAI
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-
-
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PRA isomerase
PRAI
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-
-
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additional information
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imidazole glycerol phosphate synthase mutant enzyme forms that generate phosphoribosylanthranilate isomerase activity: D130V, D130T, D130P. Mutant form of EC 5.3.1.6 that generate phosphoribosylanthranilate isomerase activity: D127V, D127K, D127T, D127G, D127F, D127V/T164H
PRA isomerase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase
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 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
CAS REGISTRY NUMBER
COMMENTARY
37259-82-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
enzyme structure
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
high catalytic efficiency
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
high catalytic efficiency
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
reaction mechanism involving general acid-base catalysis and a Schiff base intermediate, Cys-7 and Asp-126 are important for the reaction
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
enzyme structure
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
high catalytic efficiency
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ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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fourth step in tryptophan biosynthesis
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?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
imidazole glycerol phosphate synthase mutant enzyme forms that generate phosphoribosylanthranilate isomerase activity: D130V, D130T, D130P. Mutant form of EC 5.3.1.6 that generate phosphoribosylanthranilate isomerase activity: D127V, D127K, D127T, D127G, D127F, D127V/T164H
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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competitive inhibitor
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
binds reversibly
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00028
N-(5-phospho-beta-D-ribosyl)anthranilate
pH 7.5, 25°C, dimer
0.00028
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, dimer
0.00028
N-(5-phospho-beta-D-ribosyl)anthranilate
-
wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C
0.00039
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 45°C, dimer
0.00073
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 60°C, dimer
0.00103
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 80°C, dimer
0.018
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C
0.019
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.026
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6
0.03
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6
0.036
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C
0.036
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C
0.04
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase
0.041
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6
0.043
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6
0.045
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase
0.051
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6
0.053
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C
0.28
N-(5-phospho-beta-D-ribosyl)anthranilate
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in 50 mM HEPES, pH 7.5 at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
values for PRAI variants
-
0.000092
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase
0.00018
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase
0.000183
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C
0.00022
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase
0.000283
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.0012
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C
0.0013
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6
0.0017
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6
0.0023
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6
0.0027
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6
0.0086
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6
0.009
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6
0.009
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C
0.028
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C
0.032
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.522
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, dimer
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
in 50 mM HEPES, pH 7.5 at 25°C
13.5
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 45°C, dimer
38.5
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 60°C, dimer
130
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 80°C, dimer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C
0.019
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.036
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C
0.036
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C
0.053
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C
0.074
N-(5-phospho-beta-D-ribosyl)anthranilate
-
mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C
13000
N-(5-phospho-beta-D-ribosyl)anthranilate
-
in 50 mM HEPES, pH 7.5 at 25°C
13000
N-(5-phospho-beta-D-ribosyl)anthranilate
-
wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23040
-
2 * 23040, calculated from the amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop
homodimer
homodimer
-
2 * 23040, calculated from the amino acid sequence
homodimer
-
2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray structure of a complex between TrpF and its product analogue reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutationally generated monomeric PRA isomerase, comparison to PRAI dimer
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D127V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D127V/D169V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D127V/D173V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D130V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D130V/D176V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D169V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D173V
-
the mutant shows strongly reduced activity compared to the wild type enzyme
additional information
-
mutationally generated monomers of dimeric PRAI are as active as the dimer, but far more thermolabile, Pro-52/Phe-53 deletion mutant and mutants with multiple point mutations
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
95
-
dimer, strongly resistant toward inactivation up to 95°C, half-life: 21 min
additional information
additional information
structural features resonsible for the high thermostability
additional information
-
structural features resonsible for the high thermostability
additional information
-
structural features resonsible for the high thermostability
additional information
-
mutationally generated monomers of PRAI are as active as the dimer, but far more thermolabile
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thoma, R.; Hennig, M.; Sterner, R.; Kirschner, K.
Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima
Structure
8
265-276
2000
Thermotoga maritima
Sterner, R.; Kleemann, G.R.; Szadkowski, H.; Lustig, A.; Hennig, M.; Kirschner, K.
Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer
Protein Sci.
5
2000-2008
1996
Thermotoga maritima
Hennig, M.; Sterner, R.; Kirschner, K.; Jansonius, J.N.
Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability
Biochemistry
36
6009-6016
1997
Thermotoga maritima (Q56320), Thermotoga maritima
Sterner, R.; Merz, A.; Thoma, R.; Kirschner, K.
Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima
Methods Enzymol.
331
270-280
2001
Thermotoga maritima
Henn-Sax, M.; Thoma, R.; Schmidt, S.; Hennig, M.; Kirschner, K.; Sterner, R.
Two (betaalpha)8-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates
Biochemistry
41
12032-12042
2002
Thermotoga maritima (Q56320), Thermotoga maritima
Leopoldseder, S.; Claren, J.; Jurgens, C.; Sterner, R.
Interconverting the catalytic activities of (betaalpha)(8)-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysis
J. Mol. Biol.
337
871-879
2004
Thermotoga maritima
Evran, S.; Telefoncu, A.; Sterner, R.
Directed evolution of (betaalpha)8-barrel enzymes: establishing phosphoribosylanthranilate isomerisation activity on the scaffold of the tryptophan synthase alpha-subunit
Protein Eng. Des. Sel.
25
285-293
2012
Thermotoga maritima
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