2.4.2.18: anthranilate phosphoribosyltransferase
This is an abbreviated version!
For detailed information about anthranilate phosphoribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.18
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2.4.2.18
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phosphoribosyltransferases
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chorismate
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sulfolobus
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solfataricus
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phosphorylases
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indole-3-glycerol
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glutamine-dependent
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hafniae
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4.1.3.27
- 2.4.2.18
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phosphoribosyltransferases
- chorismate
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sulfolobus
- solfataricus
- phosphorylases
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indole-3-glycerol
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glutamine-dependent
- hafniae
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4.1.3.27
Reaction
Synonyms
AnPRT, anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyl transferase, anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyltransferase, anthranilate PRT, anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase, anthranilate-PP-ribose-P phosphoribosyltransferase, More, Pat, phosphoribosyl-anthranilate pyrophosphorylase, phosphoribosylanthranilate pyrophosphorylase, phosphoribosylanthranilate transferase, phosphoribosyltransferase, anthranilate, PR transferase, PRT, sAnPRT, ssAnPRT, SSO0890, ssTrpD, strpD, Trp D, TrpD, TTC1491
ECTree
2.4.2.18 anthranilate phosphoribosyltransferaseAdvanced search results
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results (Subunits
Subunits on EC 2.4.2.18 - anthranilate phosphoribosyltransferase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
monomer
monomer or dimer
equilibrium between minor, thermo-labile monomeric and major, thermo-stable dimeric state of single mutants M47D (dissociation constant, KD: 17 +/-10 microM) and I36E (KD: 0.8 +/-0.6 microM), analytical ultracentrifugation (sedimentation equilibrium)
additional information
?
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x * 72000, strain trpAB1653trpR782, SDS-PAGE
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enzyme exists in both monomeric and dimeric forms, SDS-PAGE
dimer
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homodimer, each monomer consists of 2 subdomains alpha and alpha/beta
dimer
wild-type and mutants I36E and M47D, analytical gel filtration chromatography and analytical ultracentrifugation (sedimentation equilibrium), dimerisation mediated by residues of mainly alpha helices 1, 3 and 8 of the small alpha-helical domains (one in each subunit) in head-to-head fashion
monomer
double mutant M47D/I36E, analytical gel filtration chromatography and analytical ultracentrifugation (sedimentation equilibrium), Ile36 and Met47 situated at N-terminus and C-terminus of helix 3 of the small alpha-helical domain and involved in intimate intersubunit interactions
additional information
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in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
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in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
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anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
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in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
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additional information
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anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
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additional information
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in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
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anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
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anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
Enterobacter liquefaciens
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in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
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additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
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enzyme complex is a tetramer composed of 2 molecules each of component II and II
additional information
-
anthranilate synthase-phosphoribosylanthranilate transferase complex exists in Citrobacter species in all other bacteria examined phosphoribosylanthranilate transferase and anthranilate synthase are separate enzyme molecules
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
additional information
-
in some organisms, this enzyme is part of a multifunctional protein together with one or more other components of the system for biosynthesis of tryptophan: EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, EC 5.3.1.24
