Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
-
-
-
-
anthranilate phosphoribosyl transferase
anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase
-
-
-
-
anthranilate phosphoribosyltransferase
anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase
-
-
-
-
anthranilate-PP-ribose-P phosphoribosyltransferase
-
-
-
-
phosphoribosyl-anthranilate pyrophosphorylase
-
-
-
-
phosphoribosylanthranilate pyrophosphorylase
-
-
-
-
phosphoribosylanthranilate transferase
phosphoribosyltransferase, anthranilate
-
-
-
-
AnPRT

-
anthranilate phosphoribosyl transferase

-
anthranilate phosphoribosyl transferase
-
-
anthranilate phosphoribosyl transferase
-
bifunctional enzyme EC 4.1.3.27, 2.4.2.18
anthranilate phosphoribosyltransferase

-
anthranilate phosphoribosyltransferase
-
-
phosphoribosylanthranilate transferase

-
-
-
-
phosphoribosylanthranilate transferase
-
-
sAnPRT

-
SSO0890

locus name
strpD

gene name
TrpD

-
-
-
-
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
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)
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.
2-amino-2-pentenoate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-amino-2-pentenoate + diphosphate
-
good substrate
-
-
?
2-aminoacrylate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-2-aminoacrylate + diphosphate
-
-
-
-
?
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)-enamine + diphosphate
-
-
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
-
?
ammonia + 5-phospho-alpha-D-ribose 1-diphosphate
phosphoribosyl amine + diphosphate
-
anthranilate synthase-phosphoribosyl transferase complex subunit TrpD in vitro
-
-
?
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
?
-
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
-
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
-
-
-
-
?
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
-
enzyme of tryptophan biosynthesis
-
-
-
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Hansenula henricii
-
-
-
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Hansenula henricii
-
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
-
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
-
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
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
-
-
?
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
-
-
-
-
?
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
-
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
-
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
-
enzyme of tryptophan biosynthesis
-
-
-
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
Hansenula henricii
-
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
-
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
-
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
P50384
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
P50384
catalyzes the third step in tryptophan biosynthesis
-
-
?
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
P9WFX5
-
-
-
?
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
P9WFX5
-
-
-
?
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.
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
0.0026
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
0.0224
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
0.033
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/I169T/F193S/L320M, pH 7.2, 37°C; mutant enzyme I36E/M47D/T77I/D83G/F149S, 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
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
complex
0.15
5-phospho-alpha-D-ribose 1-diphosphate
-
I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
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
0.88
5-phospho-alpha-D-ribose 1-diphosphate
Hansenula henricii
-
-
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
0.002
anthranilate
-
25°C
0.0026
anthranilate
-
40°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
0.0032
anthranilate
-
50°C
0.0035
anthranilate
-
60°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
0.0046
anthranilate
Hansenula henricii
-
-
0.005
anthranilate
-
87°C
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.
0.014 - 6
5-phospho-alpha-D-ribose 1-diphosphate
0.014 - 13.3
anthranilate
additional information
5-phospho-alpha-D-ribose 1-diphosphate
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
0.4
5-phospho-alpha-D-ribose 1-diphosphate
-
87°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; at 25°C
0.035
anthranilate
-
40°C; at 40°C
0.046
anthranilate
-
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.067
anthranilate
-
50°C; at 50°C
0.105
anthranilate
-
60°C; 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
Hansenula henricii
-
cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate
0.4
anthranilate
-
87°C; at 87°C
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; wild-type, kcat/KM: 0.0023 1/s*microM
additional information
anthranilate
-
I36E/M47D double mutant, kcat/KM: 4.8 1/s*microM; 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
-
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.
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.
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
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.
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
dimer

-
2 * 37000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
homodimer, each monomer consists of 2 subdomains alpha and alpha/beta
dimer
-
2 * 42000, SDS-PAGE
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

-
1 * 43000, SDS-PAGE
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

-
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; 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; 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; 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; 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
-
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
Hansenula henricii
-
no aggregation with other enzymes
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; 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 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; 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
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.
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.
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))
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
-
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
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.
Largen, M.; Belser, W.L.
Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes
J. Bacteriol.
121
239-249
1975
Aeromonas caviae, Citrobacter freundii, Enterobacter cloacae, Enterobacter cloacae subsp. dissolvens, Enterobacter liquefaciens, Hafnia alvei, Morganella morganii, Pectobacterium carotovorum, 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
Hansenula 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
Hansenula 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
Escherichia coli, Klebsiella aerogenes
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
Ivens, A.; Mayans, O.; Szadkowski, H.; Wilmanns, M.; Kirschner, K.
Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus
Eur. J. Biochem.
268
2246-2252
2001
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus
brenda
Kim, C.; Xuong, N.H.; Edwards, S.; Madhusudan; Yee, M.C.; Spraggon, G.; Mills, S.E.
The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum
FEBS Lett.
523
239-246
2002
Pectobacterium carotovorum
brenda
O'Gara, J.P.; Dunican, L.K.
Mutations in the trpD gene of Corynebacterium glutamicum confer 5-methyltryptophan resistance by encoding a feedback-resistant anthranilate phosphoribosyltransferase
Appl. Environ. Microbiol.
61
4477-4479
1995
Corynebacterium glutamicum
brenda
Ramos, I.; Downs, D.M.
Anthranilate synthase can generate sufficient phosphoribosyl amine for thiamine synthesis in Salmonella enterica
J. Bacteriol.
185
5125-5132
2003
Salmonella enterica
brenda
Denby, K.J.; Jason, L.J.; Murray, S.L.; Last, R.L.
ups1, an Arabidopsis thaliana camalexin accumulation mutant defective in multiple defence signalling pathways
Plant J.
41
673-684
2005
Arabidopsis thaliana
brenda
Browne, B.A.; Ramos, A.I.; Downs, D.M.
PurF-independent phosphoribosyl amine formation in yjgF mutants of Salmonella enterica utilizes the tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase
J. Bacteriol.
188
6786-6792
2006
Salmonella enterica
brenda
Marino, M.; Deuss, M.; Svergun, D.I.; Konarev, P.V.; Sterner, R.; Mayans, O.
Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus
J. Biol. Chem.
281
21410-21421
2006
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus
brenda
Schwab, T.; Skegro, D.; Mayans, O.; Sterner, R.
A rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less thermostable
J. Mol. Biol.
376
506-516
2008
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus
brenda
Schlee, S.; Deuss, M.; Bruning, M.; Ivens, A.; Schwab, T.; Hellmann, N.; Mayans, O.; Sterner, R.
Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release
Biochemistry
48
5199-5209
2009
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus
brenda
Lambrecht, J.A.; Downs, D.M.
Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and phosphoribosyl pyrophosphate
ACS Chem. Biol.
8
242-248
2013
Salmonella enterica
brenda
Schwab, T.; Sterner, R.
Stabilization of a metabolic enzyme by library selection in Thermus thermophilus
Chembiochem
12
1581-1588
2011
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus, Sulfolobus solfataricus P2 (P50384)
brenda
Mayans, O.; Ivens, A.; Nissen, L.J.; Kirschner, K.; Wilmanns, M.
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry
EMBO J.
21
3245-3254
2002
Sulfolobus solfataricus (P50384), Sulfolobus solfataricus P2 (P50384)
brenda
Cookson, T.V.; Castell, A.; Bulloch, E.M.; Evans, G.L.; Short, F.L.; Baker, E.N.; Lott, J.S.; Parker, E.J.
Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis
Biochem. J.
461
87-98
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WFX5)
brenda
Castell, A.; Short, F.L.; Evans, G.L.; Cookson, T.V.; Bulloch, E.M.; Joseph, D.D.; Lee, C.E.; Parker, E.J.; Baker, E.N.; Lott, J.S.
The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition
Biochemistry
52
1776-1787
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WFX5)
brenda
Cookson, T.V.; Evans, G.L.; Castell, A.; Baker, E.N.; Lott, J.S.; Parker, E.J.
Structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase variants reveal the conformational changes that facilitate delivery of the substrate to the active site
Biochemistry
54
6082-6092
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WFX5), Mycobacterium tuberculosis H37Rv (P9WFX5)
brenda
Kuepper, J.; Dickler, J.; Biggel, M.; Behnken, S.; Jaeger, G.; Wierckx, N.; Blank, L.M.
Metabolic engineering of Pseudomonas putida KT2440 to produce anthranilate from glucose
Front. Microbiol.
6
1310
2015
Pseudomonas putida
brenda