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Mutational analysis of substrate recognition by human arginase type I − agmatinase activity of the N130D variant
Upon mutation of Asn130 to aspartate, the catalytic activity of human arginase I was reduced to ∼ 17% of wild‐type activity, the Km value for arginine was increased ∼ 9‐fold, and the kcat/Km valueExpand
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Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group.
The interaction of Escherichia coli agmatinase (EC 3.5.3.11) with the substrate guanidinium group was investigated by kinetic and site-directed mutagenesis studies. Putrescine and guanidinium ionsExpand
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Insights into the interaction of human liver arginase with tightly and weakly bound manganese ions by chemical modification and site-directed mutagenesis studies.
Diethyl pyrocarbonate (DEPC) caused a loss in the ability of inactive subunits of wild-type and H141F mutant human liver arginase (EC 3.5.3.1) to be reactivated by Mn(2+). The effect was reversed byExpand
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Cloning and functional expression of a rodent brain cDNA encoding a novel protein with agmatinase activity, but not belonging to the arginase family.
A rat brain cDNA encoding for a novel protein with agmatinase activity was cloned and functionally expressed. The protein was expressed as a histidine-tagged fusion product with a molecular weight ofExpand
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Studies on the functional significance of a C-terminal S-shaped motif in human arginase type I: essentiality for cooperative effects.
The functional significance of a C-terminal S-shaped motif (residues 304-322) in human arginase I was explored by examining the kinetic properties of the R308A mutant and truncated speciesExpand
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Insights into the interaction of human arginase II with substrate and manganese ions by site‐directed mutagenesis and kinetic studies
To examine the interaction of human arginase II (EC 3.5.3.1) with substrate and manganese ions, the His120Asn, His145Asn and Asn149Asp mutations were introduced separately. About 53% and 95% ofExpand
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Non-chelating inhibition of the H101N variant of human liver arginase by EDTA.
Recombinant wild-type human liver arginase (EC 3.5.3.1) expressed in Escherichia coli was markedly resistant to inhibition by ethylene diamine tetraacetic acid (EDTA). In contrast, half and fullyExpand
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