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Literature summary for 3.5.3.1 extracted from

  • Steppan, J.; Ryoo, S.; Schuleri, K.H.; Gregg, C.; Hasan, R.K.; White, A.R.; Bugaj, L.J.; Khan, M.; Santhanam, L.; Nyhan, D.; Shoukas, A.A.; Hare, J.M.; Berkowitz, D.E.
    Arginase modulates myocardial contractility by a nitric oxide synthase 1-dependent mechanism (2006), Proc. Natl. Acad. Sci. USA, 103, 4759-4764.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.3.1

Inhibitors

Inhibitors Comment Organism Structure
S-(2-boronoethyl)-L-cysteine inhibition results in augmented Ca2+-dependent NO synthase activity and NO production in isolated myocytes Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion of myocyte Rattus norvegicus 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus mitochondrial isoform arginase II negatively regulates NO synthase 1 activity by limiting substrate availability in its microdomain ?
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
heart heart homogenate Rattus norvegicus
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myocyte isolated myocyte, isoform arginase II Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mitochondrial isoform arginase II negatively regulates NO synthase 1 activity by limiting substrate availability in its microdomain Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
More isolated myocyte, enzyme arginase II co-immunoprecipitates with NO synthase 1, but not with NO synthase 3 Rattus norvegicus