Dataset Information

Abu-Soud1999_HomoArginine

ABSTRACT: This model is taken from the Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51 This model shows kinetic binding of HomoArginine to neuronal nitric oxide synthase. Model shows the substrate (Homorginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and Homoarginine to form an intermediate that contains bound imidazole and homoarginine. 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: MODEL9087988095 | BioModels | 2005-01-01

REPOSITORIES: BioModels

ACCESS DATA

Publications

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

Similar Datasets

Project description:Nitric oxide (NO) is involved in all major environmental stresses. However, most of these understandings were mainly based on pharmacological study using NO modulator compounds. Recently, our studies together with others provided a new class of plant experimental system with specific in vivo NO release through constitutively overexpressing rat neuronal NO synthase (nNOS) in plants. In this study, we found that the nNOS transgenic Arabidopsis plants displayed lower level of H2O2 content, but higher levels of antioxidant enzyme activities and osmolytes under drought stress conditions. Transcriptomic analysis identified 490 and 20 genes that were differentially expressed in wild type (WT) and nNOS transgenic plants under control and drought stress conditions, respectively. Pathway analysis revealed that many genes involved in photosynthesis, cell, misc, co-factor and vitamin metabolism, major CHO metabolism, OPP and secondary metabolism were largely changed in nNOS vs. WT under control or drought stress conditions. Interestingly, CBF1/2 and 13 zinc finger family proteins, known as important family of transcription regulators in modulating several stress-responsive genes, were differentially expressed by nNOS transgenic effect. Additionally, some genes were commonly regulated by nNOS transgenic and abscisic acid (ABA) effects, indicating new insights to cross-talk between ABA and NO. Taken together, in vivo NO modulated antioxidant enzyme activities, osmolyte level, and the expression of genes involved in several pathways, thereby resulting in enhanced stress tolerance in nNOS transgenic plants. These observations might provide some insights to understand the physiological and molecular mechanisms of NO in response to drought stress in Arabidopsis. Two transgenic Arabidopsis lines (nNOS-2 and nNOS-25) with the nNOS gene under the control of the cauliflower mosaic virus (CaMV) 35S promoter, as well as Col-0 (WT), were used in this research. RNA samples from two nNOS transgenic lines were pooled for cRNA labelling and chip hybridization.

Dataset Information

Abu-Soud1999_HomoArginine

Publications

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

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure