Models

Dataset Information

0

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 Hayashi Y. et al. J Biol Chem. (1999) 274(29):20597-602. 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. This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not.. 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.

OTHER RELATED OMICS DATASETS IN: PRJNA31257PRJNA176729

SUBMITTER: Sharat Vayttaden  

PROVIDER: MODEL4780784080 | BioModels | 2005-01-01

REPOSITORIES: BioModels

altmetric image

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]

Similar Datasets

2012-03-09 | GSE36379 | GEO
2021-11-03 | PXD011886 | Pride
2012-03-09 | E-GEOD-36379 | biostudies-arrayexpress
2005-01-01 | MODEL9087766308 | BioModels
2005-12-31 | GSE2275 | GEO
2005-01-01 | MODEL9088294310 | BioModels
2005-01-01 | MODEL9088169066 | BioModels
2007-10-08 | E-GEOD-2275 | biostudies-arrayexpress
2024-09-02 | BIOMD0000000615 | BioModels
2012-08-22 | PXD000017 | Pride