DOQCS database

NCBS Home page

Accession List

Pathway List

Authorized Users

Help

News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

Molecule Parameter List for cAMP

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

*cAMP* 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	4	5	4	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
fig4_synapse	3	Network	Shared_Object_fig4_synapse, PKC, PLA2, PLCbeta, Gq, MAPK, Ras, CaMKII, CaM, PP1, PP2B, PKA, AC
This is the composite model of 4 kinases: PKC, MAPK, PKA and CaMKII and numerous regulatory pathways involved in synaptic signaling. From Bhalla US and Iyengar R. Science (1999) 283(5400):381-7.This model comes from figure 4 of that paper. Demonstration script files for generating the figures in the paper, including figure 4, are available here.

cAMP acting as a Molecule in fig4_synapse Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
cAMP	fig4_synapse Accession No. : 3	Shared_Object_ fig4_synapse Pathway No. : 19	0	1000	No

cAMP acting as a Substrate for an Enzyme in fig4_synapse Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	cAMP-PDE / PDE	fig4_synapse Accession No. : 3	AC Pathway No. : 31	19.8413	10	4	explicit E-S complex	Substrate cAMP Product AMP
2	cAMP-PDE* / PDE*	fig4_synapse Accession No. : 3	AC Pathway No. : 31	19.8413	20	4	explicit E-S complex	Substrate cAMP Product AMP
3	PDE1 / PDE1	fig4_synapse Accession No. : 3	AC Pathway No. : 31	39.7	1.667	4.0012	explicit E-S complex	Substrate cAMP Product AMP
4	CaM.PDE1 / CaM.PDE1	fig4_synapse Accession No. : 3	AC Pathway No. : 31	39.6825	10	4	explicit E-S complex	Substrate cAMP Product AMP

cAMP acting as a Product of an Enzyme in fig4_synapse Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	AC1-CaM / kenz	fig4_synapse Accession No. : 3	AC Pathway No. : 31	20	18	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
2	AC2* / kenz	fig4_synapse Accession No. : 3	AC Pathway No. : 31	20.1149	7	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
3	AC2-Gs / kenz	fig4_synapse Accession No. : 3	AC Pathway No. : 31	20	18	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
4	AC1-Gs / kenz	fig4_synapse Accession No. : 3	AC Pathway No. : 31	20	18	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
5	AC2*-Gs / kenz	fig4_synapse Accession No. : 3	AC Pathway No. : 31	60	54	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP

cAMP acting as a Substrate in a reaction in fig4_synapse 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
1	cAMP-bind-site-B 1	fig4_synapse Accession No. : 3	PKA Pathway No. : 30	54 (uM^-1 s^-1)	33 (s^-1)	Kd(bf) = 0.6111(uM)	-	Substrate R2C2 cAMP Product R2C2-cAMP
	Kf = 54 /sec/uM, Kb = 33 /sec; PKA in normal human T lymphocytes. Hasler et al (1992) FASEB J 6:2735-2741 Kd =1e-07 M for type II, 5.6e-08 M for type I; Stephen B. Smith et al (1981) PNAS, USA 78: 1591-1595 Ka1 = 2.1e+07 /M which gives Kd = 47 nM, Kan = 5e+08 /M or Kd of 2nM from Fig.7
2	cAMP-bind-site-B 2	fig4_synapse Accession No. : 3	PKA Pathway No. : 30	54 (uM^-1 s^-1)	33 (s^-1)	Kd(bf) = 0.6111(uM)	-	Substrate R2C2-cAMP cAMP Product R2C2-cAMP2
	Kf = 54 /sec/uM, Kb = 33 /sec; Same Km (1e-07M) assumed as site B1. kf/kb = 0.7e-07M*1e06/(6e05^02) = 2e-13:2.77e-12
3	cAMP-bind-site-A 1	fig4_synapse Accession No. : 3	PKA Pathway No. : 30	75 (uM^-1 s^-1)	110 (s^-1)	Kd(bf) = 1.4667(uM)	-	Substrate R2C2-cAMP2 cAMP Product R2C2-cAMP3
	Kf = 75 /sec/uM, Kb = 110 /sec; This site has higher Kd for cAMP (kinetics within bovine myocardium) Dagfinn Ogreid and Stein Ove Doskeland (1981) FEBS Lett. 129(2):287-292
4	cAMP-bind-site-A 2	fig4_synapse Accession No. : 3	PKA Pathway No. : 30	75 (uM^-1 s^-1)	32.5 (s^-1)	Kd(bf) = 0.4333(uM)	-	Substrate R2C2-cAMP3 cAMP Product R2C2-cAMP4
	Now cAMP shows effects of cooperativity and PKA has a low Kd for cAMP.

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.