2.4.2.18: anthranilate phosphoribosyltransferase
This is an abbreviated version!
For detailed information about anthranilate phosphoribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.18
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2.4.2.18
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phosphoribosyltransferases
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chorismate
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sulfolobus
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solfataricus
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phosphorylases
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indole-3-glycerol
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glutamine-dependent
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hafniae
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4.1.3.27
- 2.4.2.18
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phosphoribosyltransferases
- chorismate
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sulfolobus
- solfataricus
- phosphorylases
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indole-3-glycerol
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glutamine-dependent
- hafniae
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4.1.3.27
Reaction
Synonyms
AnPRT, anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyl transferase, anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase, anthranilate phosphoribosyltransferase, anthranilate PRT, anthranilate-5-phosphoribosylphosphate phosphoribosyltransferase, anthranilate-PP-ribose-P phosphoribosyltransferase, More, Pat, phosphoribosyl-anthranilate pyrophosphorylase, phosphoribosylanthranilate pyrophosphorylase, phosphoribosylanthranilate transferase, phosphoribosyltransferase, anthranilate, PR transferase, PRT, sAnPRT, ssAnPRT, SSO0890, ssTrpD, strpD, Trp D, TrpD, TTC1491
ECTree
2.4.2.18 anthranilate phosphoribosyltransferaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.4.2.18 - anthranilate phosphoribosyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-(2-carboxyphenylamino)-5-(3-phosphonopropoxy)benzoic acid
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2-(2-carboxyphenylamino)-5-(4-phosphonobutoxy)benzoic acid
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2-(2-carboxyphenylamino)-5-(5-phosphonopentyloxy)benzoic acid
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N-(5-phospho-D-ribosyl)-anthranilate
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tryptophan
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the enzyme is inhibited by tryptophan only in the presence of increasing amounts of stand-alone RAM domain protein SraA. Tryptophan acts as a specific inhibitor of the enzyme by binding to SraA
Zn2+
concentrations higher than 0.1 mM Zn2+ inhibit the enzyme activity (about 80% residual activity at 0.3 mM, about 65% residual activity at 0.5 mM, about 20% residual activity at 1.0 mM)
additional information
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enzyme activity is not affected by the sole addition of SraA, Trp, Ile, Leu or Ser
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anthranilate
substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity
L-tryptophan
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transferase activity of component II is only inhibitable by L-tryptophan when the component is in the complex, this inhibition does not appear to depend upon the feedback-sensitive site of complex I
L-tryptophan
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when phosphoribosyltransferase is not an aggregate with anthranilate synthase, it is not subject to tryptophan inhibition, inhibitor site is on the anthranilate synthase component
Mg2+
marked inhibition at MgCl2 concentrations higher than 0.1 mM
Mg2+
concentrations higher than 0.2 mM Mg2+ inhibit the enzyme activity (about 85% residual activity at 0.25 mM, about 70% residual activity at 0.5 mM, about 60% residual activity at 1.0 mM)
