5.3.1.24: phosphoribosylanthranilate isomerase
This is an abbreviated version!
For detailed information about phosphoribosylanthranilate isomerase, go to the full flat file.
Word Map on EC 5.3.1.24
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5.3.1.24
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indoleglycerol
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amidotransferase
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alpha8
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betaalpha8-barrels
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dual-substrate
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biotechnology
- 5.3.1.24
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indoleglycerol
-
amidotransferase
-
alpha8
-
betaalpha8-barrels
-
dual-substrate
- biotechnology
Reaction
Synonyms
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex), isomerase, phosphoribosylanthranilate, More, N-(5'-phosphoribosyl)anthranilate isomerase, N-(5'-phosphoribosyl)anthranilate isomerase/dehydratase, N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase, N-5’-phosphoribosylanthranilate isomerase, PAI, PfTrpF, phosphoribosyl anthranilate isomerase, phosphoribosyl isomerase A, phosphoribosylanthranilate isomerase, PRA isomerase, PRAI, PRAI-LoxP, PRAI[ML256-452], PriA, PurF(I198V), Trp1, Trp1p, TrpF, TrpFCtL2, TtPRAI, xPRAI
ECTree
5.3.1.24 phosphoribosylanthranilate isomeraseAdvanced search results
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Engineering on EC 5.3.1.24 - phosphoribosylanthranilate isomerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
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
Mut_L6_PRAI_WT
loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop NGQGGSGQRFD, phosphoribosylanthranilate isomerase, EC 5.3.1.24
R139N
mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied
R19A
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
S81T
mutant, steady-state Michaelis-Menten enzyme kinetic is studied
D126N/C7A
D127V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D127V/D169V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D127V/D173V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D130V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D130V/D176V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D169V
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the mutant shows strongly reduced activity compared to the wild type enzyme
D173V
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the mutant shows strongly reduced activity compared to the wild type enzyme
additional information
additional information
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PAI deletion mutant trp6 shows abnormal growth and development, isolated from Wassilewskija ecotype, which contains 4 PAI isogenes, the only active isogene in trp6 is PAI2
additional information
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insertion of the cleavage sequence of human cytomegalovirus, HCMV, protease, which is an attractive target for antiviral drug development because of its essential function in viral replication, the enzyme serves as substrate for the protease in the screening assay for small molecule inhibitors of the protease, coexpression of HCMV protease with the engineered Trp1p substrate in yeast cells results in site-specific cleavage and functional inactivation of the Trp1p enzyme, thereby leading to an arrest of cell proliferation, this growth arrest can be suppressed by the addition of validated HCMV protease inhibitors, overview
additional information
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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
