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Molecule Parameter List for PP1-active

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

*PP1-active* 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	5	0	0	1	1

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
CaMKII_2003	49	Network	Shared_Object_CaMKII_2003, CaMKII, CaM, PP1, PP2B
Model of regulation of CaMKII by Calcium, including parallel excitatory input from CaM and inhibitory input from PP1 as regulated by Calcineurin and PKA. Cell type: neuronal. Bhalla US. Biophys J. 2004 Aug;87(2):733-44.

PP1-active acting as a Molecule in CaMKII_2003 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
PP1-active	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	1.8	1000	No
Cohen et al Meth Enz 159 390-408 is main source of info conc = 1.8 uM

PP1-active acting as an Enzyme in CaMKII_2003 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PP1-active / Deph-thr286	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII-thr286-C aM Product* CaMKII-CaM
	The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35
2	PP1-active / Deph-thr305	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII* Product** CaMKII-thr286
3	PP1-active / Deph-thr306	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	5.09907	0.35	4	explicit E-S complex	Substrate CaMK-thr306 Product CaMKII
	See Cohen et al
4	PP1-active / Deph-thr286c	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII* Product** CaMK-thr306
5	PP1-active / Deph_thr286b	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII-thr286 Product CaMKII

PP1-active acting as a Substrate in a reaction in CaMKII_2003 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
Inact-PP1	CaMKII_2003 Accession No. : 49	PP1 Pathway No. : 204	499.98 (uM^-1 s^-1)	0.1 (s^-1)	Kd(bf) = 0.0002(uM)	-	Substrate I1* PP1-active Product PP1-I1*
K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4

PP1-active acting as a Product in a reaction in CaMKII_2003 Network

Name	Accession Name	Pathway Name	Kf	Kb	Kd	tau	Reagents
dissoc-PP1-I1	CaMKII_2003 Accession No. : 49	PP1 Pathway No. : 204	1 (s^-1)	0 (uM^-1 s^-1)	-	-	Substrate PP1-I1 Product I1 PP1-active
Let us assume that the equil in this case is very far over to the right. This is probably safe.

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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