Literature summary for 3.5.3.6 extracted from

Wang, M.; Basu, A.; Palm, T.; Hua, J.; Youngster, S.; Hwang, L.; Liu, H.C.; Li, X.; Peng, P.; Zhang, Y.; Zhao, H.; Zhang, Z.; Longley, C.; Mehlig, M.; Borowski, V.; Sai, P.; Viswanathan, M.; Jang, E.; Petti, G.; Liu, S.; Yang, K.; Filpula, D.
Engineering an arginine catabolizing bioconjugate: Biochemical and pharmacological characterization of PEGylated derivatives of arginine deiminase from Mycoplasma arthritidis (2006), Bioconjug. Chem., 17, 1447-1459.

Inhibitors

Inhibitors	Comment	Organism	Structure
Polyethylene glycol	binding of 12 kDa and of 20 kDa MW inhibits the enzyme activity, but does not alter the pH-dependence of the enzyme and increases the enzyme stability during storage slightly, with PEG 12k showing the higher effect	Mycoplasma arthritidis

Organism	UniProt	Comment	Textmining
Mycoplasma arthritidis	-	-	-

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
27	-	free enzyme	Mycoplasma arthritidis

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	-	Mycoplasma arthritidis

pH Minimum	pH Maximum	Comment	Organism
4.5	7	pH-profile	Mycoplasma arthritidis

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Release 2023.1 (January 2023)