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N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
-
-
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
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
-
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
-
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
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
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N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
fourth step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
third step in tryptophan biosynthesis
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
N-(5-phospho-beta-D-ribosyl)anthranilate
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
involved in tryptophan biosynthesis from chorismate
-
?
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15100
1 * 15100, multi-angle laser light-scattering
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
22900
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 2.0 microM
22900
PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 20 microM
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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
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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
brenda
Hommel, U.; Lustig, A.; Kirschner, K.
Purification and characterization of yeast anthranilate phosphoribosyltransferase
Eur. J. Biochem.
180
33-40
1989
Escherichia coli, Saccharomyces cerevisiae
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Priestle, J.P.; Gruetter, M.G.; White, J.L.; Vincent, M.G.; Kania, M; Wilson, E.; Jardetzky, T.S.; Kirschner, K.; Jansonius, J.N.
Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli
Proc. Natl. Acad. Sci. USA
84
5690-5694
1987
Escherichia coli
brenda
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
-
brenda
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
brenda
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
brenda
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)
brenda
Setiyaputra, S.; Mackay, J.P.; Patrick, W.M.
The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel fold
J. Mol. Biol.
408
291-303
2011
Escherichia coli (P00909)
brenda
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
brenda