Literature summary for 3.5.3.1 extracted from

Cox, J.D.; Cama, E.; Colleluori, D.M.; Pethe, S.; Boucher, J.L.; Mansuy, D.; Ash, D.E.; Christianson, D.W.
Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase (2001), Biochemistry, 40, 2689-2701.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
12-16 mg/ml purified recombinant wild-type enzyme and mutant H141C complexed with substrate L-arginine, reaction intermediate Nomega-hydroxy-L-arginine and analogue Nomega-hydroxy-nor-L-arginine, hanging drop vapour diffusion method, equal columns of protein and precipitant solution containing 50 mM bicine, pH 8.5 at 22°C, 12-18% PEG 8000, 5 mM MnCl2, equilibration at 4°C over 1 ml precipitant solution as reservoir, pyramidal crystals after 4 weeks, complex preparation by soaking of crystals in 18% PEG 8000, 50 bicine, pH 8.5, 5 mM MnCl2, and 5 mM of Nomega-hydroxy-L-arginine and L-arginine for 6 days, complex formation with analogue Nomega-hydroxy-nor-L-arginine affords equilibration to pH 7.5, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution	Homo sapiens

Crystallization (Comment)

Organism

12-16 mg/ml purified recombinant wild-type enzyme and mutant H141C complexed with substrate L-arginine, reaction intermediate Nomega-hydroxy-L-arginine and analogue Nomega-hydroxy-nor-L-arginine, hanging drop vapour diffusion method, equal columns of protein and precipitant solution containing 50 mM bicine, pH 8.5 at 22°C, 12-18% PEG 8000, 5 mM MnCl2, equilibration at 4°C over 1 ml precipitant solution as reservoir, pyramidal crystals after 4 weeks, complex preparation by soaking of crystals in 18% PEG 8000, 50 bicine, pH 8.5, 5 mM MnCl2, and 5 mM of Nomega-hydroxy-L-arginine and L-arginine for 6 days, complex formation with analogue Nomega-hydroxy-nor-L-arginine affords equilibration to pH 7.5, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
H141C	site-directed mutagenesis, crystal structure determination with bound substrate and reaction intermediate	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
L-arginine + H2O = L-ornithine + urea	substrate binding structure	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine + H2O	reaction intermediate is Nomega-hydroxy-L-arginine	Homo sapiens	L-ornithine + urea	-	?