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Molecule Parameter List for Ca-CaMnNOS

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

Ca-CaMnNOS 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	1	0	0	0	1

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.

Ca-CaMnNOS acting as a Molecule in  NOS_Phosph_regulation Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
Ca-CaMnNOS	NOS_Phosph_ regulation Accession No. : 20	NOS Pathway No. : 90	0	0.0016667	No

Ca-CaMnNOS acting as 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

Ca-CaMnNOS acting as a Product in a reaction in  NOS_Phosph_regulation 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_Phosph_ regulation Accession No. : 20	NOS Pathway No. : 90	3.25 (uM^-1 s^-1)	0.05 (s^-1)	Kd(bf) = 0.0154(uM)	-	Substrate CaM-Ca4 nNOS Product Ca-CaMnNOS
Those binding CaM have a high Kd, including nNOS, ~<=10nM. The binding of CaM to nNOS has been demonstrated to act as the trigger necessary for electron transfer and catalytic activity. (Marletta, Biochemistry, 1997;36:12337-12345).