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Molecule Parameter List for PLA2* | 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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | mkp1_feedback_
effects | 4 | Network |
Shared_Object_mkp1_feedback_effects, Sos, PKC,
MAPK, PLA2, Ras,
PDGFR | | This is a network involving the MAPK-PKC feedback loop with input from the PDGFR in the synapse. The distinctive feature of this model is that it includes MKP-1 induction by MAPK, and the consequent inhibitory regulation of MAPK and the feedback loop. Lots of interesting dynamics arise from this. This link provides supplementary material for the paper Bhalla US et al. Science (2002) 297(5583):1018-23. In the form of several example simulations and demos for the figures in the paper. |
PLA2* acting as a Molecule in mkp1_feedback_effects Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | PLA2* | mkp1_feedback_
effects
Accession No. : 4 | PLA2
Pathway No. : 36 | 0 | 1000 | No | | Phosphorylated PLA2. The site differs from the site phosphorylated by PKC. See Nemenoff et al 1993 JBC 268(3):1960-1964 |
PLA2* acting as a Product of an Enzyme in mkp1_feedback_effects Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | MAPK* /
MAPK* | mkp1_feedback_
effects
Accession No. : 4 | Shared_Object_
mkp1_feedback_
effects
Pathway No. : 32 | 25.641 | 20 | 4 | explicit E-S complex | Substrate
PLA2-cytosolic
Product
PLA2*
| | Km for MBP = 25 uM at 50 uM ATP, Km for ATP = 58 uM at 1mg/ml MBP (huge excess of substrate), Vmax = 4124 pmol/min/ml at a concentartion of 125 pmol/ml of enzyme. Numbers are from pp. 54 Sanghera JS, Paddon HB, Bader SA, Pelech SL. (1990) J Biol Chem. 265(1):52-7. From Nemenoff RA, Winitz S, Qian NX, Van Putten V, Johnson GL, Heasley LE. (1993) J Biol Chem. 268(3):1960-1964 - using Sanghera's 1e-4 ratio of MAPK to protein, we get k3 = 7/sec from 1000 pmol/min/mg total protein in fig 5 I take the Vmax to be higher for PLA2 given the fold activation of PLA2 by MAPK. This is actually a balance term between MAPK and the dephosphorylation step. |
PLA2* acting as a Substrate in a reaction in mkp1_feedback_effects 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 | PLA2*-Ca-act | mkp1_feedback_
effects
Accession No. : 4 | PLA2
Pathway No. : 36 | 6
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.0167(uM) | - | Substrate
Ca
PLA2*
Product
PLA2*-Ca
| | | Nemenoff et al 1993 JBC 268:1960 report a 2X to 4x activation of PLA2 by MAPK, which seems dependent on Ca as well. This reaction represents this activation. Rates are scaled to give appropriate fold activation. | | 2 | dephosphorylate-
PLA2* | mkp1_feedback_
effects
Accession No. : 4 | PLA2
Pathway No. : 36 | 0.17
(s^-1) | 0
(s^-1) | - | - | Substrate
PLA2*
Product
PLA2-cytosolic
| | | Dephosphorylation reaction to balance MAPK phosphorylation of PLA2. This is probably mediated by PP2A. Rates determined to keep the balance of phosphorylated and non-phosphorylated PLA2 reasonable. The constraining factor is the fold activation of PLA2 by MAPK. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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