3.5.1.68: N-formylglutamate deformylase
This is an abbreviated version!
For detailed information about N-formylglutamate deformylase, go to the full flat file.
Reaction
+
=
+
Synonyms
amidase, beta-citrylglutamate, beta-CGHE, beta-citryl-L-glutamate amidase, beta-citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate hydrolase, beta-citryl-L-glutamate-hydrolysing enzyme, beta-citryl-L-glutamate-hydrolyzing enzyme, beta-citrylglutamate amidase, beta-citrylglutamate amidohydrolase, citrylglutamate amidohydrolase, citrylglutamate-hydrolysing enzyme, deformylase, formylglutamate, FG hydrolase, FGase, formylglutamate amidohydrolase, formylglutamate deformylase, formylglutamate hydrolase, hydrolase, N-formylglutamate, N-formylglutamate hydrolase
ECTree
Metals Ions
Metals Ions on EC 3.5.1.68 - N-formylglutamate deformylase
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CaCl2
-
5 mM: high activation
Co2+
-
activation, most effective, 0.8 mM: 4fold activation
MnCl2
-
5 mM: most effective activation
Ca2+
-
no activation
Ca2+
-
required for full activity, can replace Mn2+ to some extent
Divalent metal ions
-
activation
Divalent metal ions
-
required
Fe2+
-
activation below 0.1 mM, slight inhibition above 0.1 mM
Mg2+
-
no activation
Mg2+
-
required for full activity, can replace Mn2+ to some extent
Mn2+
-
no activation
Mn2+
-
required for full activity
Mn2+
-
maximal activity at 0.5-1 mM
additional information
-
no activation by Cd2+
additional information
-
no activation by Ni2+, Zn2+
additional information
-
enzyme is a metalloenzyme
additional information
-
no activation by Ni2+, Zn2+
additional information
-
no activation by Cu2+