NCBS Home page
Accession List
Pathway List
Search
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.
Search in: Search for Match By


 
Result: 1 - 6 of 6 rows are displayed

Enzyme List for pathway AC (Pathway Number 278) in Accession AMPAR_CaMKII_strong_coupling (Accession Number 64)

Entries are grouped according to Pathway Number and they are alternately color coded using  and   color.
Further ordering can be done according to header.
arrow indicates that ordering is done according to ascending or descending order.
  Enzyme Molecule /

 Enzyme Activity
Pathway Name / 
Pathway No.
Km
(uM)
kcat
(s^-1)
Ratio
(k2/k3)
Enzyme TypeReagents
1 AC1-CaM /
kenz
AC

Pathway No. 278
299.9984.54Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S
Substrate: 
ATP
Product : 
cAMP
  17 Feb 2005 Halved Vmax as the amount of enzyme has been doubled to get an integer value in the spine. 18 Feb 2005. Updated Km from BRENDA: EC No 4.6.1.1 Rat Km: 0.95 mM Turnover 12/sec. Human Km: 0.3 mM 12 umol/min/mg for mammalia, turnover is 12/sec See PMID 8663304 by Dessauer and Gilman JBC 271 1996 Unfortunately turnover range is from 34 down to 0.1 in different studies, according to BRENDA.
2 AC2* /
kenz
AC

Pathway No. 278
300.00224Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S
Substrate: 
ATP
Product : 
cAMP
  Reduced Km to match expt data for basal activation of AC2 by PKC. Now k1 = 2.9e-6, k2 = 72, k3 = 18 18 Feb: Raised Km to 300 based on BRENDA data. Unlikely to make much difference, given the vast amount of ATP.
3 cAMP-PDE /
PDE
AC

Pathway No. 278
19.8411104explicit E-S complexSubstrate: 
cAMP
Product : 
AMP
  Best rates are from Conti et al Biochem 34 7979-7987 1995. Though these are for the Sertoli cell form, it looks like they carry nicely into alternatively spliced brain form. See Sette et al JBC 269:28 18271-18274 Km ~2 uM, Vmax est ~ 10 umol/min/mg for pure form. Brain protein is 93 kD but this was 67. So k3 ~10, k2 ~40, k1 ~4.2e-6
4 cAMP-PDE* /
PDE*
AC

Pathway No. 278
19.8413204explicit E-S complexSubstrate: 
cAMP
Product : 
AMP
  This form has about twice the activity of the unphosphorylated form. See Sette et al JBC 269:28 18271-18274 1994. We'll ignore cGMP effects for now.
5 PDE1 /
PDE1
AC

Pathway No. 278
39.69991.6674.0012explicit E-S complexSubstrate: 
cAMP
Product : 
AMP
  Rate is 1/6 of the CaM stim form. We'll just reduce all lf k1, k2, k3 so that the Vmax goes down 1/6.
6 CaM.PDE1 /
CaM.PDE1
AC

Pathway No. 278
39.6831104explicit E-S complexSubstrate: 
cAMP
Product : 
AMP
  Max activity ~10umol/min/mg in presence of lots of CaM. Affinity is low, 40 uM. k3 = 10, k2 = 40, k1 = (50/40) / 6e5.

 
Result: 1 - 6 of 6 rows are displayed



Database compilation and code copyright (C) 2005, 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.