2005
DOI: 10.1111/j.1742-4658.2005.04874.x
|View full text |Cite
|
Sign up to set email alerts
|

Insights into the interaction of human arginase II with substrate and manganese ions by site‐directed mutagenesis and kinetic studies

Abstract: 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% of wild‐type arginase activity were expressed by fully manganese activated species of the His120Asn and His145Asn variants, respectively. The Km for arginine (1.4–1.6 mm) was not altered and the wild‐type and mutant enzymes were essentially inactive on agmatine. In contrast, the Asn149Asp mutant expressed almost undetectab… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

1
18
0

Year Published

2006
2006
2024
2024

Publication Types

Select...
7
1
1

Relationship

1
8

Authors

Journals

citations
Cited by 19 publications
(19 citation statements)
references
References 45 publications
1
18
0
Order By: Relevance
“…ARG1 is highly expressed in the cytosol of hepatocytes and functions in nitrogen removal in the final step of the urea cycle. The ARG2 is localized in the mitochondria in all the tissues where it provides supply of ornithine for the polyamine biosynthesis (Lopez et al, 2005). Ornithine aminotransfearse (OAT; EC 2.6.1.13) catalyses the conversion of L-ornithine and a 2-oxo acid to L-glutamate 5-semialdehyde and an L-amino acid.…”
Section: Modulation Of L-arginine-arginase Metabolic Pathwaymentioning
confidence: 99%
“…ARG1 is highly expressed in the cytosol of hepatocytes and functions in nitrogen removal in the final step of the urea cycle. The ARG2 is localized in the mitochondria in all the tissues where it provides supply of ornithine for the polyamine biosynthesis (Lopez et al, 2005). Ornithine aminotransfearse (OAT; EC 2.6.1.13) catalyses the conversion of L-ornithine and a 2-oxo acid to L-glutamate 5-semialdehyde and an L-amino acid.…”
Section: Modulation Of L-arginine-arginase Metabolic Pathwaymentioning
confidence: 99%
“…The Arginase II (hArg II) gene is found on chromosome 14 (14q.24.1). Arginase II is localized in the mitochondria in tissues such as kidney, brain, and skeletal muscle, where it is thought to provide a supply of l -ornithine (L-Orn) for L-proline and polyamine biosynthesis (1). The two enzymes share 61% amino acid sequence identity and adopt a homo-trimeric structure composed of an α/β fold consisting of a parallel eight-stranded β–sheet surrounded by several helices.…”
mentioning
confidence: 99%
“…However, arginase and agmatinase are highly discriminatory between arginine and its decarboxylated derivative. Thus, the k cat / K m value is reduced about 50 000‐fold when arginine is replaced by agmatine as the substrate for rat liver arginase [21], human arginase II is practically inactive on agmatine [22], and agmatinase does not utilize arginine as a substrate [22]. One important question to ask concerns, therefore, the key structural determinants of substrate discrimination by these two enzymes, which are considered to have a common evolutionary origin [18].…”
mentioning
confidence: 99%
“…On the other hand, in contrast with Asn130 in arginase I, the corresponding Asn149 of arginase II was not found to be a ligand for the α‐carboxylate group of the transition state analog S‐ (2‐boronoethyl)‐ l ‐cysteine [4]. Nevertheless, the arginase activity of arginase II is practically lost when Asn149 is replaced with aspartate [22].…”
mentioning
confidence: 99%