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Molecule Parameter List for nNOS | The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color. | Statistics |
nNOS participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | No. of occurrences | 1 | 0 | 0 | 0 | 0 | 1 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | NOS_Iwanaga | 11 | Pathway | NOS | This model is based on Iwanaga T et al. Biochemistry (1999) 38(50):16629-35.The model features the catalytic activity of neuronal Nitric Oxide Synthase expressed in Escherichia coli in a four step reaction mechanism. The rates found in the model are used directly from their paper and have been determined from experiments performed at 25 C. |
nNOS acting as a Molecule in NOS_Iwanaga Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | nNOS | NOS_Iwanaga Accession No. : 11 | NOS Pathway No. : 65 | 0.5 | 0.0016667 | No | Neuronal Nitric Oxide Synthase. Found in the neurons, activity is dependent on CaM binding, in response to Ca levels. Molecular weight ~160 kDa. |
nNOS acting as a Substrate in a reaction in NOS_Iwanaga Network
Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated.
Kd for higher order reaction are not consider. |
Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | Ca-CaMbind-nNOS | NOS_Iwanaga Accession No. : 11 | NOS Pathway No. : 65 | 3.25 (uM^-1 s^-1) | 0.05 (s^-1) | Kd(bf) = 0.0154(uM) | - | Substrate CaM-Ca4 nNOS
Product Ca-CaM_nNOS
| Those binding CaM have a high Kd, including nNOS, ~ <=10 nM. Calcium mediated nNOS activity is required for NO synthesis. Rates from experiments... The binding of CaM to NOS has been demonstrated to act as the trigger necessary for electron transfer and catalytic activity.(Marletta, Biochemistry, 1997;36:12337-12345) |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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