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3.5.3.1: arginase

This is an abbreviated version!
For detailed information about arginase, go to the full flat file.

Word Map on EC 3.5.3.1

Reaction

L-arginine
+
H2O
=
L-ornithine
 +
Urea

Synonyms

ARG, Arg I, Arg II, ARG1, ARG2, ARGAH1, ARGAH2, ArgI, arginase, arginase 1, arginase 1a, arginase 1b, arginase 2a, arginase 2b, arginase I, arginase II, arginase type I, arginase-1, arginase-2, arginase1, arginine amidinase, arginine amidohydrolase-1, arginine amidohydrolase-2, arginine transamidinase, canavanase, human arginase type I, Kidney-type arginase, L-arginase, L-arginine amidino hydrolase, L-arginine amidinohydrolase, L-arginine amidohydrolase, L-arginine ureahydrolase, Liver-type arginase, mitochondrial arginase, More, Non-hepatic arginase, PMN arginase, recombinant human arginase I, rhArg-PEG, rhArg1, RocF, serum arginase, SmARG, tissue arginase, type II arginase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.1 arginase

Crystallization

Crystallization on EC 3.5.3.1 - arginase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on Bacillus caldovelox crystal structure. Residues D116, D120, D234, D236 and H91, H118, H133 contribute to catalysis and stability of binuclear metal center of arginase and have an important role in binding and catalytic activity in the active site
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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
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7 mg/ml purified fully active, untruncated enzyme complexed with 5 mM inhibitor S-(2-boronoethyl)-L-cysteine in 50 mM bicine, pH 8.5, 0.003 ml mixed with 0.1 ml MnCl2 and 0.003 ml precipitant solution containing 0.1 M Tris-HCl, pH 8.3-8.5, 3 M ammonium sulfate, equilibration over 1 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.3-8.5, 3 M ammonium sulfate, and 20% v/v glycerol, hanging drop vapour diffusion method at 4°C, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
D183A and D183N mutants of human arginase I complexed with 2(S)-amino-6-boronohexanoic acid are crystallized by the sitting drop vapor diffusion method at 21°C
-
in complex with inhibitors 2(S)-amino-6-boronohexanoic acid or S-(2-boronoethyl)-L-cysteine
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
in complex with inhibitors, vapor diffusion method, using 100 mM malonic acid, imidazol, boric system pH 5, and 25% or 30% (w/v) polyethylene glycol 1500 for aginase I or II, respectively
sitting drop vapour diffusion method with 0.1 M Bis-Tris-HCl (pH 5.5), 10-20% (w/v) PEG-3350
crystallization by sitting-drop vapor diffusion method at 21°C. Crystal structures of the enzyme complexed with alpha,alpha-disubstituted boronic amino-acid inhibitors
in complex with L-ornithine and inhibitors, hanging drop vapor diffusion method, using 10% (w/v) polyethylene glycol 10000, 5% (v/v) (+/-)-2-methyl-2,4-pentanediol, and 0.1 M HEPES, pH 7.3
homology modelling and molecular dynamics study on the mechanism of metal dependency. When the active site metals are removed, loss of structural integrity is observed reflected by a larger equilibration root mean square deviation for the protein when the active site metal is removed and some loss of secondary structure. An inter-monomer salt-bridge between Glu295 and Arg404 is associated with the metal dependency
in complex with the boronic acid inhibitor 2(S)-amino-6-boronohexanoic acid, to 2.15 A resolution. There are two polypeptide insertions unique to malarial arginase, a 74-residue low complexity region contained in loop L2 and an 11-residue segment contained in loop L8. Structural studies indicate that the low-complexity region is largely disordered and is oriented away from the trimer interface, its deletion does not significantly compromise enzyme activity. The loop L8 insertion is located at the trimer interface and makes several intra- and intermolecular interactions important for enzyme function
isoform arginase I in complex with inhibitor (S)-2-amino-7-oxoheptanoic acid. Inhibitor aldehyde moiety is hydrated to form the gem-diol, one hydroxyl group bridges the Mn2+ cluster and donates a hydrogen bond to D128, and the second hydroxyl group donates a hydrogen bond to E277
-
recombinant R308K mutant, X-ray diffraction structure determination and analysis at 3.0 A resolution
-
T135A rat arginase I-BEC complex and unliganded N130A rat arginase I are crystallized by the hanging drop vapor diffusion method at 4°C
recombinant arginase
-