Dataset Information

Abu-Soud1999_NMArginine

ABSTRACT: This model is taken from the Peer-reviewed publication>Husam M. Abu-Soud et al. Biochemistry 1999, 38, 12446-12451. This model shows kinetic binding of NMArginine to neuronal nitric oxide synthase. Model shows the substrate (NM-Arginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and NM-Arginine to form an intermediate that contains bound imidazole and NM-arginine. This is followed by a slower conformational change in the Im-enzyme-substrate complex that is associated with release of bound imidazole and generation of a modified enzyme-substrate complex which is detected due to spectral change. Rates approximated based on data in Table 2. The rates for first reaction are not exact since only Kd known and appropriate graphs do not exist for matching the profile. 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.

SUBMITTER: Sharat Vayttaden

PROVIDER: MODEL9088169066 | BioModels | 2005-01-01

REPOSITORIES: BioModels

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Stopped-flow analysis of substrate binding to neuronal nitric oxide synthase.

Abu-Soud H M HM Wang J J Rousseau D L DL Stuehr D J DJ

Biochemistry 19990901 38

The kinetics of binding L-arginine and three alternative substrates (homoarginine, N-methylarginine, and N-hydroxyarginine) to neuronal nitric oxide synthase (nNOS) were characterized by conventional and stopped-flow spectroscopy. Because binding these substrates has only a small effect on the light absorbance spectrum of tetrahydrobiopterin-saturated nNOS, their binding was monitored by following displacement of imidazole, which displays a significant change in Soret absorbance from 427 to 398 ...[more]

PMID: 10493814

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