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Hayashi1999_NOSynth_Phospho


ABSTRACT: This model features the phosphorylation of rat brain neuronal NOS expressed in E. coli or Sf9 cells, which leads to a decrease in Vmax of the phosphorylated enzyme, with little change of both the Km for L-arginine and Kact for CaM. This is based on <a href = "http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10400690">Hayashi Y. et al. J Biol Chem. (1999) 274(29):20597-602</a>. They report of phosphorylatin being carried out by CaM kinases I alpha, II alpha and IV. The rates used have been obtained from their paper and from other reported data.

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To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

ORGANISM(S): Rattus

SUBMITTER: Sharat Vayttaden 

PROVIDER: MODEL4780784080 | biostudies-other |

SECONDARY ACCESSION(S): 10400690

REPOSITORIES: biostudies-other

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Publications

Regulation of neuronal nitric-oxide synthase by calmodulin kinases.

Hayashi Y Y   Nishio M M   Naito Y Y   Yokokura H H   Nimura Y Y   Hidaka H H   Watanabe Y Y  

The Journal of biological chemistry 19990701 29


Phosphorylation of neuronal nitric-oxide synthase (nNOS) by Ca2+/calmodulin (CaM)-dependent protein kinases (CaM kinases) including CaM kinase Ialpha (CaM-K Ialpha), CaM kinase IIalpha (CaM-K IIalpha), and CaM kinase IV (CaM-K IV), was studied. It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at S  ...[more]

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