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Accession information for HomoArginine (Accession Number 73)

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Accession Basic Parameters

Name HomoArginine
Accession Type Pathway
Transcriber Sharat J. Vayttaden and Prasoon Agarwal, NCBS
Developer Abu-Soud HM, Wang J, Rousseau DL, and Stuehr DJ
Entry Date (YYYY-MM-DD) 2006-08-07 00:00:00
Species human
Tissue Kidney cell expressing the rat brain nNOS
Cell Compartment Cytosol
Source Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. ( Peer-reviewed publication )
Methodology Quantitative match to experiments
Model Implementation Exact GENESIS implementation
Model Validation Approximates original data
Notes 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 kinetic profile.

Conversion formats

Native Format (GENESIS format)    acc73.g   
MATLAB format    acc73.m   
SBML format    acc73.xml   

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