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anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
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anthranilate phosphoribosyl transferase
anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase
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anthranilate phosphoribosyltransferase
anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase
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anthranilate-PP-ribose-P phosphoribosyltransferase
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phosphoribosyl-anthranilate pyrophosphorylase
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phosphoribosylanthranilate pyrophosphorylase
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phosphoribosylanthranilate transferase
phosphoribosyltransferase, anthranilate
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AnPRT
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anthranilate phosphoribosyl transferase
-
anthranilate phosphoribosyl transferase
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-
anthranilate phosphoribosyl transferase
-
bifunctional enzyme EC 4.1.3.27, 2.4.2.18
anthranilate phosphoribosyltransferase
-
anthranilate phosphoribosyltransferase
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phosphoribosylanthranilate transferase
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phosphoribosylanthranilate transferase
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sAnPRT
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SSO0890
locus name
strpD
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TrpD
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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
-
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)
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
Enterobacter liquefaciens
-
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)
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)
-
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
-
enzyme is component II of the anthranilate synthase-phosphoribosyl transferase complex
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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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2-amino-2-pentenoate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-amino-2-pentenoate + diphosphate
good substrate
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?
2-aminoacrylate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminoacrylate + diphosphate
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-
-
?
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminocrotonate + diphosphate
ammonia + 5-phospho-alpha-D-ribose 1-diphosphate
phosphoribosyl amine + diphosphate
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anthranilate synthase-phosphoribosyl transferase complex subunit TrpD in vitro
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-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
additional information
?
-
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminocrotonate + diphosphate
good substrate
-
-
?
2-aminocrotonate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminocrotonate + diphosphate
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reaction product predicted to be a phosphoribosyl-enamine adduct, which breaks down directly into phosphoribosyl amine and 2-ketobutyrate (a reaction mediated by TrpD or non-enzymatic), or which breaks down non-enzymatically into ribose 5'-phosphate, 2-ketobutyrate and NH3. Ribose 5'-phosphate and NH3 combine non-enzymatically to form phosphoribosyl amine
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?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
the enzyme is required for tryptophan biosynthesis, and is involved, in coordination with several other enzymes, in defense responses of the plant, e.g. in case of pathogen infection or after treatment with acifluorfen
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Enterobacter liquefaciens
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-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Enterobacter liquefaciens
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
r
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
tryptophan biosynthesis, class III phosphoribosyltransfer
-
-
ir
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
37°C, pH 7.2, 0.05 mM Mg2+
-
-
ir
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
catalyzes the third step in tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
catalyzes the third step in tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
generation of phosphoribosyl amine from 5-phospho-alpha-D-ribose 1-diphosphate is a step in thiamine biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
reaction is catalyzed by the TrpD subunit of the anthranilate synthase-phosphoribosyl transferase complex
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
the tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase, composed of the TrpD and TrpE proteins, is essential for phosphoribosyl amine formation in strains lacking both yjgF and purF
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
also 4- and 5-carbon enamines (2-aminocrotonate, 2-amino-2-pentenoate, also 2-aminoacrylate) serve as substrates, 2-aminobutyrate is not used as substrate
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
additional information
?
-
no activity with 2-aminobutyrate
-
-
?
additional information
?
-
-
no activity with 2-aminobutyrate
-
-
?
additional information
?
-
-
connections between purine, thiamine, and tryptophan biosynthetic pathways, overview, the enzyme complex can substitute for PurF in formation of phosphoribosyl amine in vivo
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
additional information
?
-
-
connections between purine, thiamine, and tryptophan biosynthetic pathways, overview, the enzyme complex can substitute for PurF in formation of phosphoribosyl amine in vivo
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
the enzyme is required for tryptophan biosynthesis, and is involved, in coordination with several other enzymes, in defense responses of the plant, e.g. in case of pathogen infection or after treatment with acifluorfen
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Enterobacter liquefaciens
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
r
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
tryptophan biosynthesis, class III phosphoribosyltransfer
-
-
ir
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
catalyzes the third step in tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
catalyzes the third step in tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
generation of phosphoribosyl amine from 5-phospho-alpha-D-ribose 1-diphosphate is a step in thiamine biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
the tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase, composed of the TrpD and TrpE proteins, is essential for phosphoribosyl amine formation in strains lacking both yjgF and purF
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
enzyme of tryptophan biosynthesis
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00007 - 1.54
5-phospho-alpha-D-ribose 1-diphosphate
0.000005 - 0.297
anthranilate
0.00007
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme D223N
0.00016
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
0.00017
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
0.00026
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.0003
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
0.002
5-phospho-alpha-D-ribose 1-diphosphate
25°C
0.0021
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.0024
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.0026
5-phospho-alpha-D-ribose 1-diphosphate
40°C
0.0026
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme E224Q
0.0032
5-phospho-alpha-D-ribose 1-diphosphate
50°C
0.0035
5-phospho-alpha-D-ribose 1-diphosphate
60°C
0.0043
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
0.005
5-phospho-alpha-D-ribose 1-diphosphate
87°C
0.01
5-phospho-alpha-D-ribose 1-diphosphate
-
0.013
5-phospho-alpha-D-ribose 1-diphosphate
-
TAX6trpR782
0.013
5-phospho-alpha-D-ribose 1-diphosphate
mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.019
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.02
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.0224
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.023
5-phospho-alpha-D-ribose 1-diphosphate
mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.032
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.5 and 25°C
0.033
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
0.037
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
0.038
5-phospho-alpha-D-ribose 1-diphosphate
mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.045
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
0.047
5-phospho-alpha-D-ribose 1-diphosphate
wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.047
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
0.054
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
0.055
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
0.055
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.06
5-phospho-alpha-D-ribose 1-diphosphate
-
trpAB1653trpR782
0.062
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
0.085
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.086
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
complex
0.116
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.15
5-phospho-alpha-D-ribose 1-diphosphate
I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
0.15
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.151
5-phospho-alpha-D-ribose 1-diphosphate
mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.18
5-phospho-alpha-D-ribose 1-diphosphate
wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration
0.2
5-phospho-alpha-D-ribose 1-diphosphate
-
component II
0.25
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 55°C
0.371
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.88
5-phospho-alpha-D-ribose 1-diphosphate
-
-
1.54
5-phospho-alpha-D-ribose 1-diphosphate
wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.000005
anthranilate
at 87°C, Km decreases at lower temperatures
0.000018
anthranilate
wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.00002
anthranilate
wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.00004
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
0.000058
anthranilate
I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
0.00007
anthranilate
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
0.000085
anthranilate
wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration
0.00012
anthranilate
mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.00016
anthranilate
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N
0.00053
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
0.00075
anthranilate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.00091
anthranilate
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q
0.0012
anthranilate
mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.0022
anthranilate
at pH 8.5 and 55°C
0.003
anthranilate
-
TAX6trpR782
0.0031
anthranilate
mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.0036
anthranilate
mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.004
anthranilate
-
trpAB1653trpR782
0.007
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
0.008
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
0.011
anthranilate
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
0.0125
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A
0.029
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
0.037
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
0.051
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
0.06
anthranilate
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
0.082
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.149
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A
0.297
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00016 - 6
5-phospho-alpha-D-ribose 1-diphosphate
0.014 - 13.3
anthranilate
additional information
5-phospho-alpha-D-ribose 1-diphosphate
0.00016
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.00067
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.014
5-phospho-alpha-D-ribose 1-diphosphate
25°C
0.035
5-phospho-alpha-D-ribose 1-diphosphate
40°C
0.046
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.067
5-phospho-alpha-D-ribose 1-diphosphate
50°C
0.105
5-phospho-alpha-D-ribose 1-diphosphate
60°C
0.13
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.18
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.5 and 25°C
0.25
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.27
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.28
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.4
5-phospho-alpha-D-ribose 1-diphosphate
87°C
0.42
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.43
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.44
5-phospho-alpha-D-ribose 1-diphosphate
-
at pH 7.5 and 25°C
0.48
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.62
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
0.73
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A/H154A
0.78
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
1.1
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
1.2
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
1.3
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
2
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A
2.7
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
3.4
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
3.5
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
3.9
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
4.2
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
4.4
5-phospho-alpha-D-ribose 1-diphosphate
-
-
5.1
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
5.6
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme E224Q
6
5-phospho-alpha-D-ribose 1-diphosphate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme D223N
0.014
anthranilate
25°C
0.014
anthranilate
at 25°C
0.035
anthranilate
at 40°C
0.046
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.067
anthranilate
at 50°C
0.105
anthranilate
at 60°C
0.24
anthranilate
wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.28
anthranilate
+/-0.06, I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
0.33
anthranilate
wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.34
anthranilate
-
cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate
0.41
anthranilate
+/-0.04, wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration
0.48
anthranilate
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.62
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
0.73
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A
0.78
anthranilate
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
1.1
anthranilate
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
1.2
anthranilate
mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
1.2
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
1.3
anthranilate
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
2
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A
2
anthranilate
mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
2.7
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
2.9
anthranilate
-
cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate
3.4
anthranilate
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
3.5
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
3.9
anthranilate
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
4.1
anthranilate
-
cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate
4.2
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
4.4
anthranilate
mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
5.1
anthranilate
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
5.6
anthranilate
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q
6
anthranilate
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N
13.3
anthranilate
mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
additional information
5-phospho-alpha-D-ribose 1-diphosphate
I36E/M47D double mutant, kcat/KM: 0.0019 1/s*microM
additional information
5-phospho-alpha-D-ribose 1-diphosphate
-
I36E/M47D double mutant, kcat/KM: 0.0019 1/s*microM
additional information
5-phospho-alpha-D-ribose 1-diphosphate
wild-type, kcat/KM: 0.0023 1/s*microM
additional information
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, kcat/KM: 0.0023 1/s*microM
additional information
anthranilate
I36E/M47D double mutant, kcat/KM: 4.8 1/s*microM
additional information
anthranilate
-
I36E/M47D double mutant, kcat/KM: 4.8 1/s*microM
additional information
anthranilate
wild-type, kcat/KM: 4.8 1/s*microM
additional information
anthranilate
-
wild-type, kcat/KM: 4.8 1/s*microM
additional information
additional information
single mutants I36E and M47D show the same kcat as I36E/M47D double mutant within experimental error
-
additional information
additional information
-
single mutants I36E and M47D show the same kcat as I36E/M47D double mutant within experimental error
-
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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)
?
-
x * 72000, strain trpAB1653trpR782, SDS-PAGE
?
-
enzyme exists in both monomeric and dimeric forms, SDS-PAGE
?
-
x * 36000, His-tagged enzyme, SDS-PAGE
dimer
-
2 * 37000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
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
dimer
-
2 * 42000, SDS-PAGE
homodimer
-
2 * 37500, calculated from amino acid sequence
homodimer
-
2 * 41900, calculated from amino acid sequence
homodimer
2 * 36000, SDS-PAGE
homodimer
2 * 34347, calculated from amino acid sequence
monomer
-
1 * 39800, calculated from amino acid sequence
monomer
-
1 * 39800, calculated from amino acid sequence
-
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
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 38500, calculated from amino acid sequence
monomer
-
1 * 38500, calculated from amino acid sequence
-
monomer
-
1 * 39400, calculated from amino acid sequence
monomer
-
1 * 39400, calculated from amino acid sequence
-
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
-
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
-
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
-
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
-
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
-
no aggregation with other enzymes
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
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
-
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
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D223N
kcat is 5.5fold higher than wild-type value at 2 mM Mg2+
D83G
inhibition by Mg2+ only at very high concentrations, alters the binding mode of the substrate Mg2+-5-phospho-alpha-D-ribose 1-diphosphate
E224Q
kcat is 5fold higher than wild-type value at 2 mM Mg2+
F149S
is inhibited by MgCl2 to a similar extent as wild-type, facilitates product release by increasing the conformational flexibility of the enzyme
H107A
kcat is 1.2fold higher than wild-type value at 0.05 mM Mg2+
H107A/P178A
kcat is 2.1fold lower than wild-type value at 0.05 mM Mg2+
I36E
weakened intersubunit interaction and increased protein solubility by introduction of negative side chain, monomer-dimer equilibrium (dissociation constant, KD: 0.8 +/-0.6 microM), concentration-dependent kinetic stability during heat inactivation (80°C) with half-lives from 3 to 40 min, no suitable crystal formed
I36E/M47D
mutation leads to monomerization, apparent melting temperature is 11.5°C lower than the wild-type value
I36E/M47D/D83G/F149S
mutation leads to monomerization, apparent melting temperature is 21.4°C lower than the wild-type value. kcat/Km for anthranilate is 14.5fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 33fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/F193S
mutation leads to monomerization, apparent melting temperature is 17.4°C lower than the wild-type value. kcat/Km for anthranilate is 52fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 31.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/I169T
mutation leads to monomerization, apparent melting temperature is 20.6°C lower than the wild-type value. kcat/Km for anthranilate is 8.9fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 24.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/F149S/L320M
mutation leads to monomerization, apparent melting temperature is 20.9°C lower than the wild-type value. kcat/Km for anthranilate is 11fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 31.3fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/N109S/F149S
mutation leads to monomerization, apparent melting temperature is 20.5°C lower than the wild-type value. kcat/Km for anthranilate is 39fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
I36E/M47D/D83G/N109S/F149S/I169T/L320M/N324I
mutation leads to monomerization, apparent melting temperature is 18.5°C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S
mutation leads to monomerization, apparent melting temperature is 13.3°C lower than the wild-type value. kcat/Km for anthranilate is 13.3fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
I36E/M47D/T77I/D83G/F149S/F193S
mutation leads to monomerization, apparent melting temperature is 11.4°C lower than the wild-type value
I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M
mutation leads to monomerization, apparent melting temperature is 9.1°C lower than the wild-type value. kcat/Km for anthranilate is 85.7fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 2.7fold lower than kcat/Km for wild-type enzyme
I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M
mutation leads to monomerization, apparent melting temperature is 8.7°C lower than the wild-type value. kcat/Km for anthranilate is 209fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is higher than kcat/Km for wild-type enzyme
K106Q
kcat is 2.3fold lower than wild-type value at 2 mM Mg2+
M47D
weakened intersubunit interaction and increased protein solubility by introduction of negative side chain, monomer-dimer equilibrium (dissociation constant, KD: 17 +/-10 microM), concentration-dependent kinetic stability during heat inactivation (80°C) with half-lives from 4 to 15 min, no structural perturbation
M47D/I36E
double mutant, monomeric, similar catalytic efficiencies as the wild-type for both substrates, first-order kinetics for time-dependent but not concentration-dependent heat inactivation at 80°C with half-live t1/2: 3 min, no suitable crystal formed
R164A
kcat is 6.8fold lower than wild-type value at 0.05 mM Mg2+
R164A/H154A
kcat is 5.8fold lower than wild-type value at 0.05 mM Mg2+
D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 9.5°C lower than the wild-type value
-
I36E/M47D/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 21.4°C lower than the wild-type value. kcat/Km for anthranilate is 14.5fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 33fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/D83G/F149S/I169T
-
mutation leads to monomerization, apparent melting temperature is 20.6°C lower than the wild-type value. kcat/Km for anthranilate is 8.9fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 24.3fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/D83G/N109S/F149S
-
mutation leads to monomerization, apparent melting temperature is 20.5°C lower than the wild-type value. kcat/Km for anthranilate is 39fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
-
I36E/M47D/T77I/D83G/F149S
-
mutation leads to monomerization, apparent melting temperature is 13.3°C lower than the wild-type value. kcat/Km for anthranilate is 13.3fold lower than kcat/Km for wild-type enzyme. kcat/Km for anthranilate is lower than kcat/Km for wild-type enzyme. kcat/Km for 5-phospho-alpha-D-ribose 1-diphosphate is 10fold higher than kcat/Km for wild-type enzyme
-
D282A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
G308L
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
H307A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
K306A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
N309A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
P362L
-
mutation in enzyme complex subunit TrpD, increased activity compared to the wild-type enzyme
R364A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
T279A
-
mutant enzyme does not generate sufficient phosphoribosyl amine to allow growth in the absence of thiamine, mutant enzyme does synthesize sufficient tryptophan to allow growth (in vivo analysis using the Salmonella enterica strain DM9813 (purF gnd ridA trpD, auxotrophic requirement for purines, thiamine and tryptophan))
additional information
-
mutant ups1, i.e. underinducer after pathogen and stress 1, shows reduced enzyme expression and is defective in regulation of tryptophan biosynthetic enzymes and in camalexin accumulation, reduced defense against pathogen infection or after treatment with acifluorfen, phenotype and genotype analysis, overview
D83G/F149S
activity increases up to about 2-5 mM MgCl2 and decreases only moderately at higher Mg2+ concentrations
D83G/F149S
mutation leads to monomerization, apparent melting temperature is 9.5°C lower than the wild-type value
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Largen, M.; Belser, W.L.
Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes
J. Bacteriol.
121
239-249
1975
Enterobacter cloacae, Aeromonas caviae, Citrobacter freundii, Hafnia alvei, Enterobacter liquefaciens, Pectobacterium carotovorum, Enterobacter cloacae subsp. dissolvens, Morganella morganii, Proteus vulgaris, Serratia marcescens, Serratia rubidaea
brenda
Ito, J.; Yanofsky, C.
Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits
J. Bacteriol.
97
734-742
1969
Escherichia coli
brenda
Wegman, J.; DeMoss, J.A.
The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa
J. Biol. Chem.
240
3781-3788
1965
Neurospora crassa
brenda
Grieshaber, M.
On the evolution of a oligocephalic enzyme. Glutamine-chorismate-amidotransferase-free anthranilate phosphoribosyltransferases from mutant strains of Salmonella typhimurium
Z. Naturforsch. C
33c
235-244
1978
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Hommel, U.; Lustig, A.; Kirschner, K.
Purification and characterization of yeast anthranilate phosphoribosyltransferase
Eur. J. Biochem.
180
33-40
1989
Saccharomyces cerevisiae
brenda
Gonzalez, J.E.; Sommerville, R.L.
The anthranilate aggregate of Escherichia coli: kinetics of inhibition by tryptophan of phosphoribosyltransferase
Biochem. Cell Biol.
64
681-691
1986
Escherichia coli
brenda
Kane, J.F.; Jensen, R.A.
Metabolic interlock. The influence of histidine on tryptophan biosynthesis in Bacillus subtilis
J. Biol. Chem.
245
2384-2390
1970
Ogataea henricii
brenda
Bode, R.; Birnbaum, D.
Enzymes of the aromatic amino acid biosynthesis in Hansenula henricii: anthranilate phosphoribosylpyrophosphate-phosphoribosyltransferase (E.C.2.4.2.18)
Z. Allg. Mikrobiol.
18
559-566
1978
Ogataea henricii
brenda
Henderson, E.J.; Zalkin, H.; Hwang, L.H.
The anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase aggregate. Catalytic and regulatory properties of aggregated and unaggregated forms of anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
J. Biol. Chem.
245
1424-1431
1970
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Grieshaber, M.; Bauerle, R.
Monomeric and dimeric forms of component II of the anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase complex of Salmonella typhimurium. Implications concerning the mode of assembly of the complex
Biochemistry
13
373-383
1974
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Largen, M.; Mills, S.E.; Rowe, J.; Yanofsky, C.
Purification, subunit structure and partial amino-acid sequence of anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from the enteric bacterium Serratia marcescens
Eur. J. Biochem.
67
31-36
1976
Serratia marcescens
brenda
Egan, A.F.; Gibson, F.
Anthranilate synthase-anthranilate 5-phosphoribosyl 1-pyrophosphate phosphoribosyltransferase from Aerobacter aerogenes
Biochem. J.
130
847-859
1972
Klebsiella aerogenes, Escherichia coli
brenda
Marcus, S.L.; Balbinder, E.
Purification of anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase from Salmonella typhimurium using affinity chromatography: resolution of monomeric and dimeric forms
Biochem. Biophys. Res. Commun.
47
438-444
1972
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Edwards, S.E.; Kraut, J.; Xuong, N.; Ashford, V.; Halloran, T.P.; Mills, S.L.
Crystallization and purification of the enzyme anthranilate phosphoribosyl transferase
J. Mol. Biol.
203
523-524
1988
Hafnia alvei
brenda
Largen, M.; Mills, S.E.; Rowe, J.; Yanofsky, C.
Purification and properties of a third form of anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from the Enterobacteriaceae
J. Biol. Chem.
253
409-412
1978
Pectobacterium carotovorum
brenda
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