CaMKIIalpha caused the most rapid phosphorylation of nNOS, with half-maximal phosphorylation apparent at 3 min and plateau level at 10 min. (Hayashi et al., 1999,JBC,274(29):20597-20602). The Maximal Phosphorylation of nNOS was observed at ~0.4 mol of 32p/mol of nNOS under their conditions.
Activity is similar to CaMKIalpha, with ~0.7 mol of 32p/mol of nNOS. (Hayashi et 1999,JBC,274(29):20597-20602)
Hayashi et al., 1999, JBC,274(29):20597-20602. and other reported data from sources.
Phosphorylates nNOS, but not as effective as CaMKIIalpha. (Hayashi et al., 1999,JBC,274(29):20597-20602.) Report of Plateau Level in their phosphorylation plots reaching after 100 min. -- ~0.4 mol of 32p/mol of nNOS.
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.
Hayashi et al., 1999, JBC,274(29):20597-20602. and from various other datas.
Km for purified NOS is estimated between 1 - 10 uM. (Prog in Neurobiology, 2001, 64: 365-391) Vmax for unphosporylated NOS, the active form, is 500-1500 nmol/nmol/min (Montellano et al., 1998, JBC,26(12): 1185-1189). Hayashi et al., JBC, 1999, 274(29):20597-20602 report Vmax (nmol/min/mg) of nNOS Unphosporylated at 95.7 (+-) 4.2
enzyme parameters used from different literature. Hayashi et al., JBC,274(29):20597-20602.
Those binding CaM have a high Kd, including nNOS, ~<=10nM. The binding of CaM to nNOS has been demonstrated to act as the trigger necessary for electron transfer and catalytic activity. (Marletta, 1997;36:12337-12345).
kf -13.9 These rates used to keep the basal level of nNOS at reasonable levels.