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Molecule Parameter List for PIP2

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

*PIP2* 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	3	0	1	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
PLCbeta1	13	Pathway	PLCbeta
This is a model of PLCbeta1 in the bovine brain membranes as stimulated by Ca, Gq and PA. The primary data sources are Irene Litosch Biochemistry (2000) 39(26):7736-43, Sternweis PC et al. Philos Trans R Soc Lond B Biol Sci. (1992) 336(1276):35-41 and Smrcka AV et al. Science (1991) 251(4995):804-7.

PIP2 acting as a Molecule in PLCbeta1 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
PIP2	PLCbeta1 Accession No. : 13	PLCbeta Pathway No. : 67	25	0.0016667	Yes
12 Jul 2001 The PIP2 concentration is fixed to 25uM and is buffered to maitain the same level of substrate. I. Liotsch, Biochem., 2000, 39, 7736-7743.

PIP2 acting as a Substrate for an Enzyme in PLCbeta1 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	Ca.PLCbeta / Ca.PLCbeta	PLCbeta1 Accession No. : 13	PLCbeta Pathway No. : 67	10	7	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate PIP2 Product DAG IP3
	3 Nov 2001 Sternweis et al Phil Trans Soc R Lond B Biol Sci 1992 Apr 29; 336(1276);35-41;discussion 41-2. The Km and Vmax values according to Sternweis et al. The Km is fixed to 10uM since there is absence of Gq and so is the Vmax values which is fixed at 7uM since the Km obtained varies between 5 and 20uM and Vmax between 7 and 23umol/min/mg depending on the presence and absence of Gq.
2	PA.Ca.PLCbeta / PA.Ca.PLCbeta	PLCbeta1 Accession No. : 13	PLCbeta Pathway No. : 67	10	38	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate PIP2 Product DAG IP3
	3 Nov 2001 The Km and Vmax were fixed relatively to the Km and Vmax values of Ca.PLCbeta and Gq.Ca.PLCbeta which were obtained from the works of Sternweis et al and Smrcka et al where the Km varied between 5 and 20uM and Vmax between 7 and 23 umol/min/mg depending on the presence and absence of Gq.
3	Gq.Ca.PLCbeta / Gq.Ca.PLCbeta	PLCbeta1 Accession No. : 13	PLCbeta Pathway No. : 67	10	23	4	explicit E-S complex	Substrate PIP2 Product DAG IP3
	3 Nov 2001 The Km and Vmax values are fixed accordingly from Sternweis et al Phil Trans R Soc Lond B Bio Sci 1992 Apr 29;336(1276):35-41;discussion 41-2 and Smrcka et al Science 251 804-807 1991 where Km varied between 5 and 20uM and Vmax between 7 and 23 umol/min/mg depending on the presenece and absence of Gq.

PIP2 acting as a Substrate in a reaction in PLCbeta1 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
Basal	PLCbeta1 Accession No. : 13	PLCbeta Pathway No. : 67	0.009 (s^-1)	0 (uM^-1 s^-1)	-	-	Substrate PIP2 Product DAG IP3
6 Nov 2001 The basal reaction rates are fixed according to the respomse curves obtained from I. Litosch, Biochem.,2000, 39, 7736-7743.

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