DOQCS Database

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Molecule Parameter List for CaMKIV

The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network.
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Statistics

*CaMKIV* 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	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.

CaMKIV acting as a Molecule in NOS_Phosph_regulation Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CaMKIV	NOS_Phosph_ regulation Accession No. : 20	NOS Pathway No. : 90	1	0.0016667	Yes
Activity is similar to CaMKIalpha, with ~0.7 mol of 32p/mol of nNOS. (Hayashi et al., 1999,JBC,274(29):20597-20602)

CaMKIV 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
CaMKIV / kenz	NOS_Phosph_ regulation Accession No. : 20	NOS Pathway No. : 90	5	18	4	explicit E-S complex	Substrate nNOS Product NOS*
Hayashi et al., 1999, JBC,274(29):20597-20602. and other reported data from different sources.