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Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase
for references in articles please use BRENDA:EC5.3.1.24
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EC Tree 5 Isomerases
5.3 Intramolecular oxidoreductases
5.3.1 Interconverting aldoses and ketoses, and related compounds
5.3.1.24 phosphoribosylanthranilate isomerase
IUBMB 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)].
The enzyme appears in viruses and cellular organisms
- 5.3.1.24
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indoleglycerol
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amidotransferase
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alpha8
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betaalpha8-barrels
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dual-substrate
- biotechnology
Reaction Schemes
showSynonyms
prai, phosphoribosyl anthranilate isomerase, phosphoribosylanthranilate isomerase, n-(5'-phosphoribosyl)anthranilate isomerase, ttprai, pra isomerase, trpfctl2, phosphoribosyl isomerase a, trp1p, pftrpf, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
CgTrpCF
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'-phosphoribosyl)anthranilate isomerase
N-(5'-phosphoribosyl)anthranilate isomerase/dehydratase
N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
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-
-
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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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phosphoribosyl anthranilate isomerase
phosphoribosylanthranilate isomerase
PRA isomerase
PRAI
PRAI-LoxP
variant of phosphoribosylanthranilate isomerase with an insertion coding for a Cre-lox recognition site in the loop linking alpha-helix 4 and beta-stand 5
PRAI[ML256-452]
PurF(I198V)
-
the glutamine phosphoribosylpyrophosphate amidotransferase mutant I198V possesses detectable PRAI activity
TrpCF
TrpF
TrpFCtL2
TrpFGt
xPRAI
additional information
bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase
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N-(5'-phosphoribosyl)anthranilate isomerase/dehydratase
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PRA isomerase
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PRAI
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-
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PRAI
PRAI is the C-terminal domain of a bifunctional indole-3-glycerol phosphate synthase:N-(5'-phosphoribosyl)anthranilate isomerase enzyme in Escherichia coli
PRAI[ML256-452]
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engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
PRAI[ML256-452]
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engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
PRAI[ML256-452]
-
engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
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TrpF
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a (beta/alpha)8-barrel enzyme involved in the tryptophan biosynthetic pathway
TrpF
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a (beta/alpha)8-barrel enzyme involved in the tryptophan biosynthetic pathway
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xPRAI
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monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli
xPRAI
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monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli
-
additional information
see also EC 4.1.1.48, indole-3-glycerol-phosphate synthase
additional information
-
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
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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
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
catalytic mechanism
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N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
catalytic mechanism
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
catalytic mechanism
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
kinetic mechanism
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
kinetic mechanism
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
catalytic mechanism
-
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N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
kinetic mechanism
-
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Amadori rearrangement
intramolecular oxidoreduction
-
-
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-tryptophan biosynthesis
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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)].
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CAS REGISTRY NUMBER
COMMENTARY
37259-82-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
Substrates: -
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: mechanism
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: structure of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 2 well-defined functional domains: N-terminal indole-3-glycerol-phosphate synthetase, residues 1-255, and C-terminal PRA isomerase, residues 256-452, with limited noncovalent contacts between the domains, the two reactions are catalyzed independently from each other
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: structure of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 2 well-defined functional domains: N-terminal indole-3-glycerol-phosphate synthetase, residues 1-255, and C-terminal PRA isomerase, residues 256-452, with limited noncovalent contacts between the domains, the two reactions are catalyzed independently from each other
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: structure of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 2 well-defined functional domains: N-terminal indole-3-glycerol-phosphate synthetase, residues 1-255, and C-terminal PRA isomerase, residues 256-452, with limited noncovalent contacts between the domains, the two reactions are catalyzed independently from each other
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Ogataea henricii CCY 38-10-2
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Ogataea henricii CCY 38-10-2
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: mechanism
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: thermodynamic equilibrium strongly favors the product
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: mechanism
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: thermodynamic equilibrium strongly favors the product
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
Products: enolamine is the first product, which then tautomerizes to the alpha-amino ketone
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: enzyme structure
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: enzyme structure
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: high catalytic efficiency
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: high catalytic efficiency
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: high catalytic efficiency
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: reaction mechanism involving general acid-base catalysis and a Schiff base intermediate, Cys-7 and Asp-126 are important for the reaction
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: 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
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
additional information
?
-
Substrates: besides phosphoribosyl anthranilate isomerase activity, enzyme is involved in folate synthesis, reaction of EC 4.2.1.160
Products: -
Products: -
?
additional information
?
-
Substrates: besides phosphoribosyl anthranilate isomerase activity, enzyme is involved in folate synthesis, reaction of EC 4.2.1.160
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme activity of TrpFGt is determined by a coupled enzyme assay system by using the thermostable TrpD from Thermococcus kodakarensis (EC 2.4.2.18, UniProt ID Q9YGB4). Because the substrate for TrpFGt is highly unstable at higher temperatures, a continuous coupled enzyme activity assay is performed
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme activity of TrpFGt is determined by a coupled enzyme assay system by using the thermostable TrpD from Thermococcus kodakarensis (EC 2.4.2.18, UniProt ID Q9YGB4). Because the substrate for TrpFGt is highly unstable at higher temperatures, a continuous coupled enzyme activity assay is performed
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme is essential for cell proliferation in the absence of tryptophan
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
additional information
?
-
-
Substrates: the enzyme is essential for cell proliferation in the absence of tryptophan
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
Substrates: -
Products: -
Products: -
?
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Escherichia coli W3110 / ATCC 27325
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
r
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Ogataea henricii CCY 38-10-2
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: third step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Substrates: involved in tryptophan biosynthesis from chorismate
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: -
Products: -
Products: -
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: fourth step in tryptophan biosynthesis
Products: -
Products: -
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N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
Substrates: involved in tryptophan biosynthesis from chorismate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
poor effects by Co2+ and Cu2+ at 1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
guanidine hydrochloride
more than 40% decrease in activity at 2 M. The activity is completely inhibited at 6 M, at room temperature
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
competitive inhibitor
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
competitive inhibitor
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
competitive inhibitor
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
binds reversibly; competitive inhibitor
additional information
-
chemically synthesized N-(5-phospho-beta-D-ribosyl)anthranilate contains inhibitors, but not if it is generated by anthranilate phosphoribosyltransferase
-
additional information
poor inhibitory effects by Co2+ and Cu2+ at 1 mM
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthralgia
Validity and reliability of the Patient-Reported Arthralgia Inventory: validation of a newly-developed survey instrument to measure arthralgia.
Neoplasms
Validity and reliability of the Patient-Reported Arthralgia Inventory: validation of a newly-developed survey instrument to measure arthralgia.
Starvation
Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli.
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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
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
0.00115
N-(5-phospho-beta-D-ribosyl)anthranilate
recombinant enzyme, pH 8.0, 60°C
0.0032
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, recombinant xPRAI, expressed in Escherichia coli
0.004
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA, PRA isomerase activity
0.0047
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25°C, monomeric domain PRAI[ML256-452]
0.0049
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25°C, bifunctional IGPS:PRAI
0.005
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA, PRA isomerase activity
0.0083
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA mutant R19A, PRA isomerase activity
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 D169V, 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
0.04
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
-
in 50 mM HEPES, pH 7.5 at 25°C
additional information
additional information
-
increasing the pH from 7.5 to 8.6 increases the Km
-
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis, overview
-
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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
1.4
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA mutant R19A, PRA isomerase activity
3.4
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA, PRA isomerase activity
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, dimer
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
in 50 mM HEPES, pH 7.5 at 25°C
3.7
N-(5-phospho-beta-D-ribosyl)anthranilate
-
wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C
12
N-(5-phospho-beta-D-ribosyl)anthranilate
PriA, PRA isomerase activity
13.5
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 45°C, dimer
32
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25°C, monomeric domain PRAI[ML256-452]
38.5
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 60°C, dimer
40
N-(5-phospho-beta-D-ribosyl)anthranilate
-
bifunctional IGPS:PRAI
69
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25°C, recombinant xPRAI, expressed in E. coli
130
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 80°C, dimer
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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 D169V, 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
0.053
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25°C, recombinant xPRAI, expressed in Escherichia coli
0.0022
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
recombinant xPRAI, expressed in Escherichia coli
0.0065
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5
0.0065
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25°C, bifunctional IGPS:PRAI
0.0068
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25°C, monomeric domain PRAI[ML256-452]
0.0068
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
over 40% of maximal activity within this range, recombinant enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 80
over 40% of maximal activity within this range, recombinant enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
not associated with indole-3-glycerol-phosphate synthetase
-
-
brenda
strain ATCC 13137, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional enzyme, additionally catalyes the reaction of EC 4.2.1.160
UniProt
brenda
bifunctional enzyme, additionally catalyes the reaction of EC 4.2.1.160
UniProt
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
Ogataea henricii CCY 38-10-2
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
SwissProt
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
indole-3-glycerol-phosphate synthetase and PRA isomerase form an easily dissociable multienzyme complex
-
-
brenda
multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase
-
-
brenda
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
bifunctional N-(5-phosphoribosyl)anthranilate isomerase/indole-3-glycerolphosphate synthase, cf. EC 4.1.1.48
UniProt
brenda
bifunctional N-(5-phosphoribosyl)anthranilate isomerase/indole-3-glycerolphosphate synthase, cf. EC 4.1.1.48
UniProt
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
a fragment of the beta subunit of the multifunctional alpha2beta2 anthranilate synthetase complex has PRA isomerase and indole-3-glycerol phosphate synthetase activities, organization of the functional domains of the compex
-
-
brenda
component IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities
-
-
brenda
multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase
-
-
brenda
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase
-
-
brenda
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
brenda
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
ecotype Columbia, expression patterns of the 3 PAI isogenes, which are differentially regulated under normal growth conditions and differentially expressed in a tissue- and cell-type-specific manner
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis
metabolism
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
metabolism
-
in microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme. L-Tryptophan biosynthetic pathway, overview
-
physiological function
enzyme TrpFCtL2, in combination with GTP cyclohydrolase II, i.e. RibA, the first enzyme of riboflavin synthesis, provides a bypass of the first two canonical steps in folate synthesis catalyzed by FolE and FolQ. TrpFCtL2 retains the phosphoribosyl anthranilate isomerase activity of the original annotation
physiological function
expression of Trp1 gene complements the Trp1 mutation in Saccharomyces cerevisiae
physiological function
phosphoribosyl anthranilate isomerase is involved in the isomerization of phosphoribosyl anthranilate to 1-(ocarboxyphenylamino)-1-deoxyribulose 5-phosphate
physiological function
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
enzyme TrpFCtL2, in combination with GTP cyclohydrolase II, i.e. RibA, the first enzyme of riboflavin synthesis, provides a bypass of the first two canonical steps in folate synthesis catalyzed by FolE and FolQ. TrpFCtL2 retains the phosphoribosyl anthranilate isomerase activity of the original annotation
-
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
TrpCF is a bifunctional enzyme that has indole-glycerol-phosphate synthase (IGPS) and phosphoribosylanthranilate isomerase (PRAI) activity. In microorganisms, L-tryptophan biosynthesis involves five steps catalyzed by the enzymes of seven different genes. Among the enzymes, phosphoribosylanthranilate isomerase (PRAI, TrpF) is an enzyme that catalyzes the Amadori rearrangement from N-(5'-phosphoribosyl)anthranilate (PRA) to 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CdRP) as the third step in the biosynthesis process. Indole-glycerol-phosphate synthase (IGPS, TrpC) is an enzyme that catalyzes reaction from CdRP to indole-3-glycerol-phosphate (IGP) through a ring closure reaction in the fourth step. These two enzymes are encoded by one gene and expressed as a bifunctional enzyme
-
physiological function
-
phosphoribosyl anthranilate isomerase is involved in the isomerization of phosphoribosyl anthranilate to 1-(ocarboxyphenylamino)-1-deoxyribulose 5-phosphate
-
additional information
three-dimensional structural modeling of enzyme TrpFGt using the previously reported crystal structures of phosphoribosyl anthranilate isomerase from Thermotoga maritima (1NSJ) and Escherichia coli (1PII) as templates
additional information
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
active site structure determination by attaching rCdRP similar to the substrate and product of the TrpCF reaction. The enzyme shows a conformational change at the loops upon substrate binding, molecular docking simulation using IGP docking to the CgTrpCF structure, detailed overall structure of CgTrpCF, overview
-
additional information
-
three-dimensional structural modeling of enzyme TrpFGt using the previously reported crystal structures of phosphoribosyl anthranilate isomerase from Thermotoga maritima (1NSJ) and Escherichia coli (1PII) as templates
-
Show AA Sequence and Transmembrane Helices (19185 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
-
component IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities, gel filtration
185000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
22900
23000
23040
-
2 * 23040, calculated from the amino acid sequence
45000
46000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, sedimentation equilibrium
47000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
48000
49400
49500
-
1 * 49500, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, amino acid sequence analysis
49800
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 100 microM, deduced association state dimer
53000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
56000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit, gel filtration
22900
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 2.0 microM
22900
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 20 microM
23000
-
monomeric domain PRAI[ML256-452], gel filtration and analytical ultracentrifugation
45000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
45000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
48000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
48000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
48000
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
49400
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
49400
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
49400
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
-
the indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit exists as a dimer
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
homodimer
2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop
monomer
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
monomer
-
1 * 49500, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, amino acid sequence analysis
monomer
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
monomer
Escherichia coli W3110 / ATCC 27325
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
monomer
Escherichia coli W3110 / ATCC 27325
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
-
monomer
thermodynamically stable and entropically optimized monomeric TIM-barrel enzyme
monomer
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
monomer
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
monomer
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
monomer
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
-
additional information
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
-
secondary structure analysis of the bifunctional enzyme, detailed analysis from the crystal structure, overview
-
additional information
crystallographic analysis suggests that TrpF is unable to form a dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 resolution, respectively. TrpCF shows a conformational change at the loops upon substrate binding
purified recombinant C-terminally His6-tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 52 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution, containing 0.8 M potassium sodium tartrate tetrahydrate and 0.1 M sodium-HEPES, pH 7.5, and equilibration against 0.05 ml of reservoir solution, 2 days, 20°C, method optimization, X-ray diffraction structure determination and analysis at 2.10-2.21 A resolution. Crystals of CgTrpCF in complex with rCdRP are crystallized in different concentrations of protein (35.4 mg/ml with addition of 3 mM reduced 1-(2-carboxyphenylamino)-1-deoxyribulose 5-phosphate). The crystals of CgTrpCF in the complex form appear in 22% PEG 3350 and 0.2 M magnesium chloride hexahydrate
three-dimensional structure of indole-3-glycerol-phosphate synthetase/PRA isomerase complex determined by X-ray crystallography
-
hanging-drop vapour-diffusion experiments at room temperature, crystallizes in space group P6(1), structure is determined at 1.75 A resolution
hanging-drop vapour-diffusion method, crystallized using the hanging-drop method in 1.5 M ammonium sulfate and 100 mM sodium citrate pH 4.8. Crystals are obtained up to 0.05 * 0.05 * 0.3 mM size, space group P3(1,2)21, unit cell parameters a = 65.1 A, c = 104.7 A
-
the structure of the PriA mutant R139N is determined to a resolution of 1.95 A
hanging drop vapor diffusion method
mutationally generated monomeric PRA isomerase, comparison to PRAI dimer
-
x-ray structure
X-ray structure of a complex between TrpF and its product analogue reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E290A
mutation in isomerase domain, about 65% of wild-type catalytic activity
E290V
H338Y
mutation in synthase domain, about 10% of wild-type catalytic activity
I391L
mutation in synthase domain, about 35% of wild-type catalytic activity
I391V
mutation in synthase domain, about 100% of wild-type catalytic activity
P294K
E290A
Mut_L2_FBPA
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop SNGGASFIAGKGVKSDVPQ, fructose-bisphosphate aldolase, EC 4.1.2.13
Mut_L2_MR
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop GYPAL, mandelate racemase, EC 5.1.2.2
Mut_L2_PRAI_WT
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop VATSPRCVN, phosphoribosylanthranilate isomerase, EC 5.3.1.24
Mut_L2_Ure
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop GGTGPAAGTHATTCTPG, urease, EC 3.5.1.5
Mut_L4_ADA
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop GDELGFPGSLF, adenosine diaminase, EC 3.5.4.4
Mut_L4_alphaTS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop DVPVQQS, tryptophan synthase, EC 4.2.1.20
Mut_L4_DHDPS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop PYYNRPS, dihydrodipicolinate synthase, EC 4.2.1.52
Mut_L4_FBPA
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop DLSEES, fructose-bisphosphate aldolase, EC 4.1.2.13
Mut_L4_MR
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop EPTLEHD, mandelate racemase, EC 5.1.2.2
Mut_L4_PBGS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop AAMDG, porphobilinogen synthase, EC 4.2.1.24
Mut_L4_PRAI_WT
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop GNEE, phosphoribosylanthranilate isomerase, EC 5.3.1.24
Mut_L4_TPS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop LGQEDLH, thiamine-phosphate diphosphorylase, EC 2.5.1.3
Mut_L4_Ure
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop EDWGAT, urease, EC 3.5.1.5
Mut_L6_alphaTS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop SRAGVTGAENRAALP, tryptophan synthase, EC 4.2.1.20
Mut_L6_DHDPS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop TGNL, dihydrodipicolinate synthase, EC 4.2.1.52
Mut_L6_PBGS
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop PAGAY, porphobilinogen synthase, EC 4.2.1.24
Mut_L6_PRAI_WT
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop NGQGGSGQRFD, phosphoribosylanthranilate isomerase, EC 5.3.1.24
R139N
mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied
R19A
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
S81T
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
D126N/C7A
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
E290V
mutation in synthase domain, about 120% of wild-type catalytic activity
E290V
site-directed mutagenesis, the residues of the substrate-binding site in TrpCF are highly conserved except for some residues. These less conserved residues (e.g. Glu290, Pro294, His338, and Ile391) are replaced, the resulting CgTrpCFE290V mutant has enhanced enzyme activity compared to wild-type enzyme. The replacement of Glu290 by Val might increase the hydrophobic interaction with the aromatic ring of the anthranilate moiety
P294K
mutation in synthase domain, about 175% of wild-type catalytic activity
P294K
site-directed mutagenesis, the residues of the substrate-binding site in TrpCF are highly conserved except for some residues. These less conserved residues (e.g. Glu290, Pro294, His338, and Ile391) are replaced, the resulting CgTrpCFP294K mutant has enhanced enzyme activity compared to wild-type enzyme. The replacement of Pro294 by Lys might enable the residue to form a salt bridge with the carboxyl group of the anthranilate moiety
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
E290A
-
mutation in isomerase domain, about 65% of wild-type catalytic activity
-
additional information
-
PAI deletion mutant trp6 shows abnormal growth and development, isolated from Wassilewskija ecotype, which contains 4 PAI isogenes, the only active isogene in trp6 is PAI2
additional information
-
insertion of the cleavage sequence of human cytomegalovirus, HCMV, protease, which is an attractive target for antiviral drug development because of its essential function in viral replication, the enzyme serves as substrate for the protease in the screening assay for small molecule inhibitors of the protease, coexpression of HCMV protease with the engineered Trp1p substrate in yeast cells results in site-specific cleavage and functional inactivation of the Trp1p enzyme, thereby leading to an arrest of cell proliferation, this growth arrest can be suppressed by the addition of validated HCMV protease inhibitors, overview
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
-
25°C, 16 h, most stable in potassium phosphate buffer, in presence of 1 mM dithioerythritol
additional information
additional information
denaturation at acidic pH is correlated with the dissociation of its dimeric form
additional information
-
denaturation at acidic pH is correlated with the dissociation of its dimeric form
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48 - 50
-
the melting temperatures of wild type TrpF are 48 and 50°C when the protein concentrations are 0.002 and 0.02 mM, respectively
60
purified recombinant enzyme, half-life is 90 min
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified recombinant enzyme TrpFGt is highly stable against protein denaturants such as urea at room temperature. There is no significant change in activity even after treatment with 8M urea. While Gdn-HCl leads to more 40% decrease in activity even at 2 M at room temperature. The activity is completely inhibited at 6 M
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
very susceptible to autooxidation catalyzed by Cu2+ and other heavy metal ions, oxidation is prevented by EDTA and dithioerythritol
-
648872
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.8 M sucrose, 7 days, 20% loss of activity, 15 days, 65% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a nickel Sepharose column, HisTrap FF, and a gel-filtration column, Sephacryl S200, are used
component IIb of the anthranilate synthetase complex, purified from trp2 mutant
-
functional, recombinant, soluble enzyme 4.7fold from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by heate treatment of the soluble fraction, followed by anion exchange chromatography, dialysis, and another different step of anion exchange chromatography
indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit
-
Ni-NTA column chromatography, HiTrap Q column chromatography, Superdex 200 gel filtration
-
partial
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of trpF mutants, expression in Escherichia coli BL21(DE3)
gene trpCF, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)-T1
gene trpFGt, DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant expression of the soluble enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIL
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase
-
separation of the 2 domains of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex on the gene level, expression of monofunctional PRAI[ML256-452] in Escherichia coli W3110 trpR, deltatrp EA2
-
sequence of trpCF gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
the expression of PRAI-LoxP variants is performed in Escherichia coli Rosetta 2 cells transformed with pET28b+ plasmids containing the encoding sequences
TRP1 gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complex is cloned, expressed in Escherichia coli and sequenced
TRP1 gene encoding multifunctional enzyme is cloned in Escherichia coli and sequenced
-
TRPC gene encoding multifunctional enzyme is cloned in Escherichia coli and sequenced
-
trpF gene is cloned and expressed in Escherichia coli
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
the work provides a method of exchanging variably sized loops within the (beta/alpha)8 fold, affording a novel starting point for the screening of novel activities as well as modest diversions from an original activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoch, S.O.
Isolation and characterization of two tryptophan biosynthetic enzymes, indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase, from Bacillus subtilis
J. Bacteriol.
139
362-368
1979
Bacillus subtilis, Bacillus subtilis T3
brenda
Largen, M.; Belser, W.L.
Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes
J. Bacteriol.
121
239-249
1975
Citrobacter freundii, Aeromonas caviae, Proteus vulgaris, Pectobacterium carotovorum, Serratia rubidaea, Citrobacter freundii NCTC 6021, Pectobacterium carotovorum ICPB EC153
brenda
Potts, J.M.; Drapeau, G.R.
Partial characterization of phosphoribosyl transferase, phosphoribosyl anthranilate isomerase, and indole glycerol phosphate synthase from Serratia marcescens
J. Bacteriol.
111
334-339
1972
Serratia marcescens, Serratia marcescens HY
brenda
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Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI
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Escherichia coli, Saccharomyces cerevisiae
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Aspergillus nidulans, Coprinopsis lagopus, Coprinopsis radiata, Escherichia coli, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe
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Hommel, U.; Eberhard, M.; Kirschner, K.
Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reaction
Biochemistry
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Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI
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Biochemistry
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Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Priestle, J.P.; Gruetter, M.G.; White, J.L.; Vincent, M.G.; Kania, M; Wilson, E.; Jardetzky, T.S.; Kirschner, K.; Jansonius, J.N.
Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli
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The TRP1 gene of Phytophora parasitica encoding indole-3-glycerolphosphate synthase-N-(5'-phossphoribosyl)anthranilate isomerase: structure and evolutionary distance from homologous fungal genes
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Phytophthora nicotianae (P24920)
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Thermotoga maritima
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Arabidopsis thaliana
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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
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Thermotoga maritima (Q56320), Thermotoga maritima
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Thermotoga maritima (Q56320), Thermotoga maritima
brenda
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Expression, purification and preliminary crystallographic analysis of phosphoribosyl isomerase (PriA) from Streptomyces coelicolor
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Streptomyces coelicolor
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Metarhizium anisopliae (Q873X5), Metarhizium anisopliae
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Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments
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Thermus thermophilus HB8 (P83825), Thermus thermophilus HB8
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Thermotoga maritima
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Cottier, V.; Barberis, A.; Luethi, U.
Novel yeast cell-based assay to screen for inhibitors of human cytomegalovirus protease in a high-throughput format
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Saccharomyces cerevisiae
brenda
Patrick, W.M.; Matsumura, I.
A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase
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Escherichia coli
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Experimental evidence for the existence of a stable half-barrel subdomain in the (beta/alpha)8-barrel fold
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Escherichia coli, Escherichia coli M15
brenda
Ochoa-Leyva, A.; Soberon, X.; Sanchez, F.; Argueello, M.; Montero-Moran, G.; Saab-Rincon, G.
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Escherichia coli (P00909)
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Noda-Garcia, L.; Camacho-Zarco, A.R.; Verdel-Aranda, K.; Wright, H.; Soberon, X.; Fueloep, V.; Barona-Gomez, F.
Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (beta alpha)8 phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activity
Protein Sci.
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Streptomyces coelicolor (P16250), Streptomyces coelicolor
brenda
Setiyaputra, S.; Mackay, J.P.; Patrick, W.M.
The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel fold
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Escherichia coli (P00909)
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Akanuma, S.; Yamagishi, A.
Roles for the two N-terminal (beta/alpha) modules in the folding of a (beta/alpha)8-barrel protein as studied by fragmentation analysis
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2011
Escherichia coli
brenda
Repo, H.; Oeemig, J.S.; Djupsjbacka, J.; Iwai, H.; Heikinheimo, P.
A monomeric TIM-barrel structure from Pyrococcus furiosus is optimized for extreme temperatures
Acta Crystallogr. Sect. D
68
1479-1487
2012
Pyrococcus furiosus (Q8U092), Pyrococcus furiosus
brenda
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
brenda
Reisinger, B.; Bocola, M.; List, F.; Claren, J.; Rajendran, C.; Sterner, R.
A sugar isomerization reaction established on various (betaalpha)8-barrel scaffolds is based on substrate-assisted catalysis
Protein Eng. Des. Sel.
25
751-760
2012
Thermotoga maritima
brenda
Adams, N.E; Thiaville, J.J; Proestos, J.; Juarez-Vazquez, A.L.; McCoy, A.J.; Barona-Gomez, F.; Iwata-Reuyl, D.; de Crecy-Lagard, V.; Maurelli, A.T.
Promiscuous and adaptable enzymes fill "holes" in the tetrahydrofolate pathway in Chlamydia species
mBio
5
e01378-14
2014
Chlamydia trachomatis (B0B7P4), Chlamydia trachomatis ATCC VR-902B (B0B7P4)
brenda
Perveen, S.; Rashid, N.; Papageorgiou, A.
Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis
Acta Crystallogr. Sect. F
72
804-812
2016
Thermococcus kodakarensis (Q9YGB1)
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brenda
Park, E.H.; Kim, M.D.
Isolation of the phosphoribosyl anthranilate isomerase gene (TRP1) from starch-utilizing yeast Saccharomycopsis fibuligera
J. Microbiol. Biotechnol.
25
1324-1327
2015
Saccharomycopsis fibuligera (A0A0H4BJU5), Saccharomycopsis fibuligera
brenda
Park, W.; Son, H.F.; Lee, D.; Kim, I.K.; Kim, K.J.
Crystal structure and functional characterization of the bifunctional N-(5-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Corynebacterium glutamicum
J. Agric. Food Chem.
69
12485-12493
2021
Corynebacterium glutamicum (P06560), Corynebacterium glutamicum ATCC 13032 (P06560), Corynebacterium glutamicum DSM 20300 (P06560), Corynebacterium glutamicum JCM 1318 (P06560), Corynebacterium glutamicum LMG 3730 (P06560), Corynebacterium glutamicum NCIMB 10025 (P06560), Corynebacterium glutamicum BCRC 11384 (P06560)
brenda
Arif, M.; Bashir, Q.; Siddiqui, M.A.; Rashid, N.
Molecular characterization of a highly efficient and thermostable phosphoribosyl anthranilate isomerase from Geobacillus thermopakistaniensis
Protein Expr. Purif.
166
105523
2020
Geobacillus thermopakistaniensis (A0A7U9P5F5), Geobacillus thermopakistaniensis MAS1 (A0A7U9P5F5)
brenda
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