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Molecule Parameter List for Larg | 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 |
Larg 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 | 1 | 0 | 0 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | NOS_Phosph_ regulation | 20 | Pathway | NOS | 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 experimental data. |
Larg acting as a Molecule in NOS_Phosph_regulation Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | Larg | NOS_Phosph_ regulation Accession No. : 20 | NOS Pathway No. : 90 | 100 | 0.0016667 | No | |
Larg acting as a Substrate for an Enzyme in NOS_Phosph_regulation Network
Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Ca-CaMnNOS / kenz | NOS_Phosph_ regulation Accession No. : 20 | NOS Pathway No. : 90 | 10 | 16.667 | 4 | explicit E-S complex | Substrate Larg
Product NO cit
| 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 |
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