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Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase and Organism(s) Escherichia coli and UniProt Accession P00909

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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)].
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Escherichia coli
UNIPROT: P00909
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
prai, phosphoribosyl anthranilate isomerase, phosphoribosylanthranilate isomerase, n-(5'-phosphoribosyl)anthranilate isomerase, pra isomerase, ttprai, trpfctl2, trp1p, pftrpf, phosphoribosyl isomerase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-(5'-phosphoribosyl)anthranilate isomerase
-
phosphoribosylanthranilate isomerase
-
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
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)
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-
-
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isomerase, phosphoribosylanthranilate
-
-
-
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N-(5'-phosphoribosyl)anthranilate isomerase
-
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N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase
-
-
-
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N-5’-phosphoribosylanthranilate isomerase
-
-
-
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PAI
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-
-
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PRA isomerase
PRAI[ML256-452]
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engineered monofunctional variant of IGPS:PRAI, excised monomeric domain
PurF(I198V)
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the glutamine phosphoribosylpyrophosphate amidotransferase mutant I198V possesses detectable PRAI activity
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
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intramolecular oxidoreduction
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-
-
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Amadori rearrangement
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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)].
CAS REGISTRY NUMBER
COMMENTARY hide
37259-82-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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product inhibition
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047 - 0.007
N-(5-phospho-beta-D-ribosyl)anthranilate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
32 - 50
N-(5-phospho-beta-D-ribosyl)anthranilate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065 - 0.0068
reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.78
-
37°C
98.7
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monofunctional domain PRAI[ML256-452]
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15100
1 * 15100, multi-angle laser light-scattering
22900
24100
PRAI-LoxP, theoretical
49800
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 100 microM, deduced association state dimer
23000
-
monomeric domain PRAI[ML256-452], gel filtration and analytical ultracentrifugation
23100
-
calculated from amino acid sequence
46000
-
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, sedimentation equilibrium
48000
-
1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE
49370
-
1 * 49370, calculated from the amino acid sequence
49400
-
1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex
49500
-
1 * 49500, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, amino acid sequence analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
-
PROTEIN VARIANTS
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
25°C, 16 h, most stable in potassium phosphate buffer, in presence of 1 mM dithioerythritol
648875
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is resistant to protease attack
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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
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648872
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, under argon, months, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a nickel Sepharose column, HisTrap FF, and a gel-filtration column, Sephacryl S200, are used
Ni-NTA agarose column chromatography and Superdex 75 gel filtration
best isolated from mutant trp A2
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HisTrap FF nickel affinity column chromatography
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indole-3-glycerol-phosphate synthetase/PRA isomerase complex
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monomeric domain PRAI[ML256-452] and bifunctional IGPS:PRAI
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Ni-NTA column chromatography
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Ni-NTA column chromatography, HiTrap Q column chromatography, Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
the expression of PRAI-LoxP variants is performed in Escherichia coli Rosetta 2 cells transformed with pET28b+ plasmids containing the encoding sequences
expressed in Escherichia coli M15 (pREP4) cells
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expressed in Escherichia coli XL1-Red cells
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overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis
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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
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sequence of trpCF gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complex
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eberhard, M.; Tsai-Pflugfelder, M.; Bolewska, K.; Hommel, U.; Kirschner, K.
Indoleglycerol phosphate synthase - phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains
Biochemistry
34
5419-5428
1995
Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI
Manually annotated by BRENDA team
Hommel, U.; Lustig, A.; Kirschner, K.
Purification and characterization of yeast anthranilate phosphoribosyltransferase
Eur. J. Biochem.
180
33-40
1989
Escherichia coli, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Creighton, T.E.; Yanofsky, C.
Chorismate to tryptophan (Escherichia coli) - anthranilate synthethase, PR transferase; PRA isomerase, InGP synthetase, tryptophan synthetase
Methods Enzymol.
17A
365-380
1970
Escherichia coli
-
Manually annotated by BRENDA team
Huetter, R.; Niederberger, P.; DeMoss, J.A.
Tryptophan biosynthetic genes in eukaryotic microorganisms
Annu. Rev. Microbiol.
40
55-77
1986
Aspergillus nidulans, Saccharomyces cerevisiae, Coprinopsis lagopus, Coprinopsis radiata, Escherichia coli, Neurospora crassa, Schizosaccharomyces pombe
Manually annotated by BRENDA team
Kirschner, K.; Szadkowski, H.; Jardetzky, T.S.; Hager, V.
Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli
Methods Enzymol.
142
386-397
1987
Acinetobacter calcoaceticus, Aspergillus nidulans, Bacillus subtilis, Escherichia coli, Escherichia coli W3110 / ATCC 27325, Neurospora crassa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, [Brevibacterium] flavum
Manually annotated by BRENDA team
Hommel, U.; Eberhard, M.; Kirschner, K.
Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reaction
Biochemistry
34
5429-5439
1995
Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI
Manually annotated by BRENDA team
Bisswanger, H.; Kirschner, K.; Cohn, W.; Hager, V.; Hansson, E.
N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A Substrate analogue binds to two different binding sites on the bifunctional enzyme from Escherichia coli
Biochemistry
18
5946-5953
1979
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team
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
Proc. Natl. Acad. Sci. USA
84
5690-5694
1987
Escherichia coli
Manually annotated by BRENDA team
White, J.L.; Gruetter, M.G.; Wilson, E.; Thaller, C.; Ford, G.C.; Smit, J.D.G.; Jansonius, J.N.; Kirschner, K.
Crystallization and preliminary X-ray crystallographic data of the bifunctional enzyme phosphoribosyl-anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli
FEBS Lett.
148
87-90
1982
Escherichia coli
-
Manually annotated by BRENDA team
Patrick, W.M.; Matsumura, I.
A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase
J. Mol. Biol.
377
323-336
2008
Escherichia coli
Manually annotated by BRENDA team
Akanuma, S.; Yamagishi, A.
Experimental evidence for the existence of a stable half-barrel subdomain in the (beta/alpha)8-barrel fold
J. Mol. Biol.
382
458-466
2008
Escherichia coli, Escherichia coli M15
Manually annotated by BRENDA team
Ochoa-Leyva, A.; Soberon, X.; Sanchez, F.; Argueello, M.; Montero-Moran, G.; Saab-Rincon, G.
Protein design through systematic catalytic loop exchange in the (beta/alpha)8 fold
J. Mol. Biol.
387
949-964
2009
Escherichia coli (P00909)
Manually annotated by BRENDA team
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
J. Mol. Biol.
408
291-303
2011
Escherichia coli (P00909)
Manually annotated by BRENDA team
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
Proteins
79
221-231
2011
Escherichia coli
Manually annotated by BRENDA team