| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
1 | PKA_dash_active / phosph_dash_PDE
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 7.5 | 9 | 4 | explicit E-S complex | Substrate cAMP_dash_PDE
Product cAMP_dash_PDE_ star
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2 | PKA_dash_active / Src_phospho
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.05 | 20 | 4 | explicit E-S complex | Substrate Src
Product Src_star
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3 | PKA_dash_active / PKA_dash_ phosph_dash_GEF
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 7.5 | 9 | 4 | explicit E-S complex | Substrate inact_dash_GEF
Product inact_dash_GEF_ star
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| This pathway inhibits Ras when cAMP is elevated. See: Hordijk et al JBC 269:5 3534-3538 1994 Burgering et al EMBO J 12:11 4211-4220 1993 The rates are the same as used in PKA-phosph-I1 |
4 | PKA_dash_active / PKA_dash_ phosph_dash_I1
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 7.5 | 9 | 4 | explicit E-S complex | Substrate I1
Product I1_star
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| #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta. |
5 | PKA_dash_active / CaMKKphosph
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 4.6999 | 0.6833 | 3.99997073156 | explicit E-S complex | Substrate CaMKK_CaM_Ca_c
Product CaMKKp CaM_dash_Ca4
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6 | PKA_dash_active / SIK2_phosp
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 4.5997 | 0.1 | 4 | explicit E-S complex | Substrate SIK2
Product SIK2_star
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