Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase

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

EC NUMBER
COMMENTARY
5.3.1.24
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylanthranilate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
catalytic mechanism; kinetic mechanism
-
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
catalytic mechanism
Q56320
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
catalytic mechanism; kinetic mechanism
Saccharomyces cerevisiae xPRAI
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Amadori rearrangement
-
-
Amadori rearrangement
Hansenula henricii
-
-
Amadori rearrangement
-
-
Amadori rearrangement
Escherichia coli W3110
-
;
-
Amadori rearrangement
Hansenula henricii CCY 38-10-2
-
-
-
Amadori rearrangement
Saccharomyces cerevisiae xPRAI
-
;
-
intramolecular oxidoreduction
-
-
-
-
isomerization
P16250
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
tryptophan biosynthesis
-
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)].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
-
-
-
-
N-(5'-phosphoribosyl)anthranilate isomerase
-
-
N-(5'-phosphoribosyl)anthranilate isomerase
P00909
-
N-(5'-phosphoribosyl)anthranilate isomerase
-
-
N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
-
-
-
-
N-5-phosphoribosylanthranilate isomerase
-
-
-
-
PAI
-
-
-
-
PfTrpF
Q8U092
-
phosphoribosyl anthranilate isomerase
P16250
-
phosphoribosyl anthranilate isomerase
-
-
phosphoribosyl isomerase A
P16250
-
phosphoribosylanthranilate isomerase
-
-
PRA isomerase
-
-
-
-
PRA isomerase
-
-
PRA isomerase
P16250
-
PRAI
-
-
-
-
PRAI
P00909
PRAI is the C-terminal domain of a bifunctional indole-3-glycerol phosphate synthase:N-(5'-phosphoribosyl)anthranilate isomerase enzyme in Escherichia coli
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]
-
engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
PRAI[ML256-452]
Saccharomyces cerevisiae xPRAI
-
engineered monofunctional variant of IGPS:PRAI, excised monomeric domain; engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
-
PurF(I198V)
-
the glutamine phosphoribosylpyrophosphate amidotransferase mutant I198V possesses detectable PRAI activity
TrpF
-
a (beta/alpha)8-barrel enzyme involved in the tryptophan biosynthetic pathway
xPRAI
-
monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli
xPRAI
Saccharomyces cerevisiae xPRAI
-
monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli; monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli
-
isomerase, phosphoribosylanthranilate
-
-
-
-
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
CAS REGISTRY NUMBER
COMMENTARY
37259-82-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
not associated with indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
strain ATCC 13137, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
ecotype Columbia, ecotype Wassilewskija
-
-
Manually annotated by BRENDA team
not associated with indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
not associated with indole-3-glycerol-phosphate synthetase; strain T3
-
-
Manually annotated by BRENDA team
Bacillus subtilis T3
strain T3
-
-
Manually annotated by BRENDA team
indole-3-glycerol-phosphate synthetase and PRA isomerase form an easily dissociable multienzyme complex
-
-
Manually annotated by BRENDA team
strain NCTC 6021, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
Citrobacter freundii NCTC 6021
strain NCTC 6021, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex; strain W3110
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
strain M15
UniProt
Manually annotated by BRENDA team
strain M15
UniProt
Manually annotated by BRENDA team
Escherichia coli W3110
strain W3110
-
-
Manually annotated by BRENDA team
Hansenula henricii
strain CCY 38-10-2, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
Hansenula henricii CCY 38-10-2
strain CCY 38-10-2, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
component IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities; multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
strain ICPB EC153, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
Pectobacterium carotovorum ICPB EC153
strain ICPB EC153, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
SwissProt
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
not associated with indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
naturally monofunctional enzyme
-
-
Manually annotated by BRENDA team
naturally monofunctional enzyme; xPRAI
-
-
Manually annotated by BRENDA team
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase
-
-
Manually annotated by BRENDA team
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; transformant strain RH218 (YARp1)
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae xPRAI
xPRAI
-
-
Manually annotated by BRENDA team
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
multifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex; strain HY
-
-
Manually annotated by BRENDA team
Serratia marcescens HY
strain HY
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
monofunctional enzyme
Uniprot
Manually annotated by BRENDA team
monofunctional enzyme; Protein Data Bank: 1NSJ
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
P16250
phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P00909
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Hansenula henricii
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P24920, -
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P16250
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
mechanism
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
show the reaction diagram
-
enzyme structure
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Q56320
enzyme structure
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
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
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
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
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
thermodynamic equilibrium strongly favors the product
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
show the reaction diagram
Q56320
high catalytic efficiency
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Q56320, -
high catalytic efficiency
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
high catalytic efficiency
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Q56320, -
reaction mechanism involving general acid-base catalysis and a Schiff base intermediate, Cys-7 and Asp-126 are important for the reaction
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Hansenula henricii
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Q56320, -
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P24920, -
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
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
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Hansenula henricii CCY 38-10-2
-
-, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Pectobacterium carotovorum ICPB EC153
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Bacillus subtilis T3
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Bacillus subtilis T3
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Serratia marcescens HY
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Serratia marcescens HY
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae xPRAI
-
-, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae xPRAI
-
mechanism, thermodynamic equilibrium strongly favors the product
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
show the reaction diagram
Saccharomyces cerevisiae xPRAI
-
third step in tryptophan biosynthesis, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli W3110
-
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
-
ir
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli W3110
-
fourth step in tryptophan biosynthesis, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli W3110
-
-, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Citrobacter freundii NCTC 6021
-
-
-
?
additional information
?
-
-
the enzyme is essential for cell proliferation in the absence of tryptophan
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P16250
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Hansenula henricii
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Q56320, -
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
P24920, -
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Hansenula henricii CCY 38-10-2
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Bacillus subtilis T3
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Serratia marcescens HY
-
involved in tryptophan biosynthesis from chorismate
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae xPRAI
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae xPRAI
-
third step in tryptophan biosynthesis, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli W3110
-
fourth step in tryptophan biosynthesis, involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
Escherichia coli W3110
-
involved in tryptophan biosynthesis from chorismate
-
?
additional information
?
-
-
the enzyme is essential for cell proliferation in the absence of tryptophan
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
product inhibition
CoCl2
Hansenula henricii
-
0.001 mM, 20% inhibition
CuSO4
Hansenula henricii
-
0.001 mM, 100% inhibition
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
-
MnCl2
Hansenula henricii
-
0.001 mM, 45% inhibition
additional information
-
not inhibited by indoleglycerol phosphate
-
additional information
-
chemically synthesized N-(5-phospho-beta-D-ribosyl)anthranilate contains inhibitors, but not if it is generated by anthranilate phosphoribosyltransferase
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00028
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, dimer
0.00028
-
N-(5-phospho-beta-D-ribosyl)anthranilate
Q56320
pH 7.5, 25C, dimer
0.00028
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, dimer
0.00028
-
N-(5-phospho-beta-D-ribosyl)anthranilate
Q56320
pH 7.5, 25C, dimer
0.00039
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 45C, dimer
0.00073
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 60C, dimer
0.00103
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 80C, dimer
0.0032
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, recombinant xPRAI, expressed in Escherichia coli
0.004
0.005
N-(5-phospho-beta-D-ribosyl)anthranilate
-
30C
0.004
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA, PRA isomerase activity
0.0047
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, monomeric domain PRAI[ML256-452]
0.0047
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, monomeric domain PRAI[ML256-452]; pH 7.5
0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, bifunctional IGPS:PRAI
0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, bifunctional IGPS:PRAI; pH 7.5
0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
-
0.0049
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, bifunctional IGPS:PRAI; pH 7.5
0.005
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA, PRA isomerase activity
0.007
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 20C
0.0083
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA mutant R19A, PRA isomerase activity
0.026
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127G, mutant form of EC 5.3.1.6
0.03
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127K, mutant form of EC 5.3.1.6
0.04
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D130P, mutant form of imidazole glycerol phosphate synthase
0.041
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127F, mutant form of EC 5.3.1.6
0.043
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127T, mutant form of EC 5.3.1.6
0.045
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D130T, mutant form of imidazole glycerol phosphate synthase
0.051
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127V/T164H, mutant form of EC 5.3.1.6
0.074
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127V, mutant form of EC 5.3.1.6; pH 7.5, 25C, D130V, mutant form of imidazole glycerol phosphate synthase
1.3
-
N-(5-phospho-beta-D-ribosyl)anthranilate
Hansenula henricii
-
pH 7.6
additional information
-
additional information
-
increasing the pH from 7.5 to 8.6 increases the Km
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000092
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D130T, mutant form of imidazole glycerol phosphate synthase
0.00018
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D130V, mutant form of imidazole glycerol phosphate synthase
0.00022
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D130P, mutant form of imidazole glycerol phosphate synthase
0.0013
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127G, mutant form of EC 5.3.1.6
0.0017
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127K, mutant form of EC 5.3.1.6
0.0023
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127F, mutant form of EC 5.3.1.6
0.0027
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127T, mutant form of EC 5.3.1.6
0.0086
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127V, mutant form of EC 5.3.1.6
0.009
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, D127V/T164H, mutant form of EC 5.3.1.6
1.4
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA mutant R19A, PRA isomerase activity
3.4
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA, PRA isomerase activity
3.7
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, dimer
3.7
-
N-(5-phospho-beta-D-ribosyl)anthranilate
Q56320
pH 7.5, 25C, dimer
12
-
N-(5-phospho-beta-D-ribosyl)anthranilate
P16250
PriA, PRA isomerase activity
13.5
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 45C, dimer
32
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, monomeric domain PRAI[ML256-452]
32
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C, monomeric domain PRAI[ML256-452]; pH 7.5
38.5
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 60C, dimer
39
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 20C
40
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
25C; bifunctional IGPS:PRAI
40
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
bifunctional IGPS:PRAI
40
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
bifunctional IGPS:PRAI; pH 7.5, 25C
50
60
N-(5-phospho-beta-D-ribosyl)anthranilate
-
30C
50
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
-
69
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 25C, recombinant xPRAI, expressed in E. coli
130
-
N-(5-phospho-beta-D-ribosyl)anthranilate
-
pH 7.5, 80C, dimer
additional information
-
additional information
-
values for PRAI variants
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0017
-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, 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
-
25C, bifunctional IGPS:PRAI
-
0.0065
-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, bifunctional IGPS:PRAI; pH 7.5
-
0.0068
-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, monomeric domain PRAI[ML256-452]
-
0.0068
-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, monomeric domain PRAI[ML256-452]; pH 7.5
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0071
-
Hansenula henricii
-
pH 7.6
5.15
-
-
-
5.5
-
-
37C, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
8.78
-
-
37C
98.7
-
-
monofunctional domain PRAI[ML256-452]
additional information
-
-
-
additional information
-
-
values for PRAI variants
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
7.5
-
Q56320
assay at
7.5
-
P16250
activity assay
7.6
-
Hansenula henricii
-
-
8.6
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q56320
assay at
25
-
P16250
activity assay
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
transgenic, ecotype Columbia
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22900
-
-
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 20 microM; PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 2.0 microM
23000
-
-
monomeric domain PRAI[ML256-452], gel filtration and analytical ultracentrifugation
23000
-
-
gel filtration
23100
-
P00909
calculated from amino acid sequence
24100
-
-
PRAI-LoxP, theoretical
26300
-
-
gel filtration
30200
-
-
dimer, gel filtration
45000
-
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
46000
-
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, sedimentation equilibrium
47000
-
-
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
49600
-
-
dimer, sedimentation equilibrium 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
160000
-
-
component IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities, gel filtration
185000
-
Hansenula henricii
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration
additional information
-
-
MWs of PRAI variants
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
active form
dimer
-
the indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit exists as a dimer
dimer
Q56320
-
dimer
P83825, -
-
dimer
P00909
-
homodimer
-
2 * 23040, calculated from the amino acid sequence; 2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop
homodimer
Q56320
2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop
homodimer
-
2 * 23040, calculated from the amino acid sequence
monomer
-
1 * 21800, SDS-PAGE
monomer
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
monomer
-
separate monomeric enzyme
monomer
-
1 * 49370, calculated from the amino acid sequence; 1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
monomer
-
separate monomeric enzyme
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 * 49500, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, amino acid sequence analysis
monomer
-
1 * 15100, multi-angle laser light-scattering
monomer
-
x-ray crystallography
monomer
-, Q8U092
thermodynamically stable and entropically optimized monomeric TIM-barrel enzyme
monomer
Bacillus subtilis T3
-
1 * 21800, SDS-PAGE
-
monomer
Escherichia coli W3110
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE; 1 * 49370, calculated from the amino acid sequence; 1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
monomer
Serratia marcescens HY
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated seeding technique; three-dimensional structure of indole-3-glycerol-phosphate synthetase/PRA isomerase complex determined by X-ray crystallography
-
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
-, Q8U092
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
P16250
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method; X-ray structure of a complex between TrpF and its product analogue reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Q56320
mutationally generated monomeric PRA isomerase, comparison to PRAI dimer
-
x-ray structure
-
oil microbatch method
P83825, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.2
-
-
strongly resistant toward inactivation by acidification to pH 3.2
6.5
7.5
-
25C, 16 h, most stable in potassium phosphate buffer, in presence of 1 mM dithioerythritol
additional information
-
-
extremely stable towards acidic pH
additional information
-
P83825, -
denaturation at acidic pH is correlated with the dissociation of its dimeric form
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48
50
P00909
the melting temperatures of wild type TrpF are 48 and 50C when the protein concentrations are 0.002 and 0.02 mM, respectively
85
-
-
dimer, half-life: 310 min; monomeric variants, half-life: 3-5 min
85
-
-
dimer, half-life: 310 min
91.5
-
-
dimer, half-life: 50 min
95
-
-
dimer, strongly resistant toward inactivation up to 95C, half-life: 21 min
additional information
-
-
extremely thermostable; mutationally generated monomers of PRAI are as active as the dimer, but far more thermolabile
additional information
-
Q56320
structural features resonsible for the high thermostability
additional information
-
-
structural features resonsible for the high thermostability
additional information
-
Q56320
extremely thermostable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10-15% v/v glycerol stabilizes
-
enzyme is resistant to protease attack
-
extremely stable enzyme
-
extremely stable towards proteolytic attack
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
very susceptible to autooxidation catalyzed by Cu2+ and other heavy metal ions, oxidation is prevented by EDTA and dithioerythritol
-
648872
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 0.8 M sucrose, 7 days, 20% loss of activity, 15 days, 65% loss of activity
-
4C, 10-15% v/v glycerol, 6-15 days, average of 24% loss of activity
-
4C, under argon, months, stable
-
4C, 24h, 35% loss of activity
Hansenula henricii
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a nickel Sepharose column, HisTrap FF, and a gel-filtration column, Sephacryl S200, are used
-
best isolated from mutant trp A2; indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
HisTrap FF nickel affinity column chromatography
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
monomeric domain PRAI[ML256-452] and bifunctional IGPS:PRAI
-
Ni-NTA agarose column chromatography and Superdex 75 gel filtration
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography, HiTrap Q column chromatography, Superdex 200 gel filtration
P00909
21fold
Hansenula henricii
-
component IIb of the anthranilate synthetase complex, purified from trp2 mutant
-
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit
-
partial
-
recombinant xPRAI, expressed in Escherichia coli
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 70fold
-
mutationally generated monomeric PRA isomerase
-
recombinant PRAI, expressed in Escherichia coli
-
TrpF mutants C7A, D126N and C7A/D126N double mutant
Q56320
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ecotype Columbia, 3 PAI isogenes: PAI1, PAI2 and PAI3
-
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; TRPC gene encoding multifunctional enzyme is cloned in Escherichia coli and sequenced
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli M15 (pREP4) cells
-
expressed in Escherichia coli XL1-Red cells
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
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
-
trpDFEG gene cluster, trpF gene encodes PRA isomerase
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis; TRP1 gene encoding multifunctional enzyme is cloned in Escherichia coli and sequenced
-
TRP1 gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complex is cloned, expressed in Escherichia coli and sequenced
P24920, -
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; TRP1 gene is cloned in Escherichia coli and sequenced
-
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; TRP1 gene regulation, cloning
-
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
-
into the vector pET-15b
P16250
cloning of trpF mutants, expression in Escherichia coli BL21(DE3)
-
trpF gene is cloned and expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
R139N
P16250
mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied
R19A
P16250
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
S81T
P16250
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
C7A
Q56320
catalytically inactive mutant
D126N
Q56320
mutant with drastically reduced 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
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
additional information
P24920, -
insertion mutagenesis of TRP1 gene
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
D126N/C7A
-
catalytically inactive double mutant
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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