Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase

New: Word Map on EC 5.3.1.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
5.3.1.24
-
RECOMMENDED NAME
GeneOntology No.
phosphoribosylanthranilate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Amadori rearrangement
intramolecular oxidoreduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-tryptophan biosynthesis
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
tryptophan metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].
CAS REGISTRY NUMBER
COMMENTARY hide
37259-82-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
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
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
Chlamydia trachomatis serovar L2
bifunctional enzyme, additionally catalyes the reaction of EC 4.2.1.160
UniProt
Manually annotated by BRENDA team
Chlamydia trachomatis serovar L2 ATCC VR-902B
bifunctional enzyme, additionally catalyes the reaction of EC 4.2.1.160
UniProt
Manually annotated by BRENDA team
strain NCTC 6021, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
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
strain M15
UniProt
Manually annotated by BRENDA team
strain W3110
-
-
Manually annotated by BRENDA team
-
-
-
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
strain ICPB EC153, bifunctional 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
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
SwissProt
Manually annotated by BRENDA team
-
-
-
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
-
SwissProt
Manually annotated by BRENDA team
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
strain HY
-
-
Manually annotated by BRENDA team
bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
show the reaction diagram
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one
7,8-dihydroneopterin 3'-phosphate + H2O
show the reaction diagram
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
additional information
?
-
-
the enzyme is essential for cell proliferation in the absence of tryptophan
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
MnCl2
Hansenula henricii
-
0.001 mM, 45% inhibition
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00028 - 1.3
N-(5-phospho-beta-D-ribosyl)anthranilate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000092 - 130
N-(5-phospho-beta-D-ribosyl)anthranilate
additional information
additional information
Thermotoga maritima
-
values for PRAI variants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 13000
N-(5-phospho-beta-D-ribosyl)anthranilate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.0068
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0071
Hansenula henricii
-
pH 7.6
5.5
-
37C, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
98.7
-
monofunctional domain PRAI[ML256-452]
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
Hansenula henricii
-
-
8.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
Escherichia coli (strain K12)
Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / CIP 55134)
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22900
-
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 2.0 microM; PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 20 microM
23100
calculated from amino acid sequence
24100
-
PRAI-LoxP, theoretical
26300
-
gel filtration
30200
-
dimer, gel filtration
46000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, sedimentation equilibrium
47000
-
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
COMMENTARY hide
LITERATURE
homodimer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
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
-
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
mutationally generated monomeric PRA isomerase, comparison to PRAI dimer
-
x-ray structure
-
oil microbatch method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2
-
strongly resistant toward inactivation by acidification to pH 3.2
648887
6.5 - 7.5
-
25C, 16 h, most stable in potassium phosphate buffer, in presence of 1 mM dithioerythritol
648875
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48 - 50
the melting temperatures of wild type TrpF are 48 and 50C when the protein concentrations are 0.002 and 0.02 mM, respectively
91.5
-
dimer, half-life: 50 min
95
-
dimer, strongly resistant toward inactivation up to 95C, half-life: 21 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
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
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
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, 24h, 35% loss of activity
Hansenula henricii
-
4C, under argon, months, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
21fold
Hansenula henricii
-
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
-
component IIb of the anthranilate synthetase complex, purified from trp2 mutant
-
HisTrap FF nickel affinity column chromatography
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 70fold
-
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit
-
monomeric domain PRAI[ML256-452] and bifunctional IGPS:PRAI
-
mutationally generated monomeric PRA isomerase
-
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
partial
recombinant PRAI, expressed in Escherichia coli
-
recombinant xPRAI, expressed in Escherichia coli
-
TrpF mutants C7A, D126N and C7A/D126N double mutant
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of trpF mutants, expression in Escherichia coli BL21(DE3)
-
ecotype Columbia, 3 PAI isogenes: PAI1, PAI2 and PAI3
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli M15 (pREP4) cells
-
expressed in Escherichia coli XL1-Red cells
-
expression in Escherichia coli
Chlamydia trachomatis serovar L2
into the vector pET-15b
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; separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; TRP1 gene is cloned in Escherichia coli and sequenced
-
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
-
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
-
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; TRP1 gene regulation, cloning
-
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
trpDFEG gene cluster, trpF gene encodes PRA isomerase
-
trpF gene is cloned and expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
C7A
catalytically inactive mutant
D126N
mutant with drastically reduced activity
D126N/C7A
-
catalytically inactive double mutant
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
D176V
-
inactive
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Show AA Sequence (7588 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.