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Result: 1 - 7 of 7 rows are displayed

Reaction List for pathway PKA (Pathway Number 196) in Accession PKA_2003 (Accession Number 47)

Entries are grouped according to Pathway Number and they are alternately color coded using  and  color.
Further ordering can be done to the table header.  indicates that ordering is done according to ascending or descending order.
Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules]
  Reaction
Name		Pathway Name / 
Pathway No.		KfKbKdtauReagents
1 
  • cAMP-bind-site-A
    1
    		• PKA

    Pathway No. 196    		75
    (uM^-1 s^-1)    		110
    (s^-1)    		Kd(bf) = 1.4667(uM)-  Substrate:
     cAMP2.R2C2
     cAMP

     Products:
     cAMP3.R2C2
    2 
  • cAMP-bind-site-A
    2
    		• PKA

    Pathway No. 196    		75
    (uM^-1 s^-1)    		32.5
    (s^-1)    		Kd(bf) = 0.4333(uM)-  Substrate:
     cAMP
     cAMP3.R2C2

     Products:
     cAMP4.R2C2
    3 Release-C1PKA

    Pathway No. 196    		60
    (s^-1)    		18
    (uM^-1 s^-1)    		Kd(cb) = 0.3(uM)-  Substrate:
     cAMP4.R2C2

     Products:
     PKA-active
     cAMP4.R2C
      This has to be fast, as the activation of PKA by cAMP is also fast. kf was 10
    4 Release-C2PKA

    Pathway No. 196    		60
    (s^-1)    		18
    (uM^-1 s^-1)    		Kd(cb) = 0.3(uM)-  Substrate:
     cAMP4.R2C

     Products:
     PKA-active
     cAMP4.R2
    5 inhib-PKAPKA

    Pathway No. 196    		60
    (uM^-1 s^-1)    		1
    (s^-1)    		Kd(bf) = 0.0167(uM)-  Substrate:
     PKA-active
     PKA-inhibitor

     Products:
     inhibited-PKA
      This has to be set to zero for matching the expts in vitro. In vivo we need to consider the inhibition though.
    6 
  • cAMP-bind-site-B
    1
    		• PKA

    Pathway No. 196    		54
    (uM^-1 s^-1)    		33
    (s^-1)    		Kd(bf) = 0.6111(uM)-  Substrate:
     R2C2
     cAMP

     Products:
     cAMP.R2C2
      Hasler et al (1992 jun) FASEB J. 6(9):2735-41 say Kd =1e-7M for type II, 5.6e-8 M for type I.
    Take mean which comes to 2e-13 #/cell Smith et al (1981 Mar) Proc Natl Acad Sci U S A 78(3) 1591-1595 have better data.
    First kf/kb=2.1e7/M = 3.5e-5 (#/cell).Ogreid and Doskeland (1981 Jul 6) FEBS Lett 129(2) 287-292 have figs suggesting time course of complete assoc is < 1 min.
    7 
  • cAMP-bind-site-B
    2
    		• PKA

    Pathway No. 196    		54
    (uM^-1 s^-1)    		33
    (s^-1)    		Kd(bf) = 0.6111(uM)-  Substrate:
     cAMP.R2C2
     cAMP

     Products:
     cAMP2.R2C2
      For now let us set this to the same Km (1e-7M) as site B. This gives kf/kb = .7e-7M * 1e6 / (6e5^2) : 1/(6e5^2) = 2e-13:2.77e-12 Smith et al (1981 Mar) Proc Natl Acad Sci U S A 78(3) 1591-1595 have better values.
    They say that this is cooperative, so the consts are now kf/kb =8.3e-4
     
    Result: 1 - 7 of 7 rows are displayed


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