2.3.1.192: glycine N-phenylacetyltransferase
This is an abbreviated version!
For detailed information about glycine N-phenylacetyltransferase, go to the full flat file.
Reaction
Synonyms
AAC, arylacetyl acyl-CoA:amino acid N-acyltransferase, arylacetyl-CoA N-acyltransferase, arylacetyltransferase, GAT, phenylacetyltransferase
ECTree
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Inhibitors
Inhibitors on EC 2.3.1.192 - glycine N-phenylacetyltransferase
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5,5'-dithiobis(2-nitrobenzoate)
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phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation
K2SO4
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55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration
Mg2+
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1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration
CoA
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at physiologic concentrations of substrate, the arylacetyl transferase is extensively inhibited by CoA, inhibition is greatly reduced by ions. The 3-phosphate group on CoA is important for binding to the salt-free enzyme but in the presence of ions its importance is diminished
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110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration. Inhibition results in a large decrease in the affinity of the enzyme for phenylacetyl-CoA. In the presence of KCl the KD values for phenylacetyl-CoA and naphthylacetyl-CoA are similar, but the KD for glycine is extremely high for 1-naphthylacetyl-CoA conjugation
KCl
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80 mM KC1, ca. 30% inhibition, inhibition is seen at all concentrations of glutamine up to 150 mM