Literature summary for 3.5.3.1 extracted from

Di Costanzo, L.; Ilies, M.; Thorn, K.J.; Christianson, D.W.
Inhibition of human arginase I by substrate and product analogues (2010), Arch. Biochem. Biophys., 496, 101-108.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitors N-hydroxy-L-arginine and nor-N-hydroxy-L-arginine, to 2.04 and 1.55 A resolution, respectively, and in complex with L-lysine, to 1.9 A resolution. Enzyme forms hydrogen bond interactions with inhibitor alpha-carboxylate and alpha-amino groups	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
L-lysine	binds to isoform arginase I with Kd of 13.1 microM	Homo sapiens
Nomega-hydroxy-L-arginine	i.e. NOHA, binds to isoform arginase I with Kd of 3.6 microM	Homo sapiens
Nomega-hydroxy-nor-L-arginine	i.e. nor-NOHA, binds to isoform arginase I with Kd of 517 nM, surface plasmon resonance, or Kd of 50 nM, isothermal titration calorimetry	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05089	-	-

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Release 2023.1 (January 2023)