Michaelis constant

(Difference between revisions)
 Revision as of 16:35, 6 December 2018 (view source)← Older edit Latest revision as of 17:51, 6 December 2018 (view source)Nnjm2 (Talk | contribs) (Removed some stray code. Cleaned up the text. Cleaned up the references.) Line 1: Line 1: − Michaelis constant is the substrate concentration at which the reaction velocity is equal to half the maximal velocity of the reaction. + Michaelis constant is the substrate concentration at which the reaction velocity is equal to half the maximal velocity of the reaction. − Km = Michaelis constant + Km = Michaelis constant Km = the value of substrate concentration[S] that causes V= ½ Vmax * Km = the value of substrate concentration[S] that causes V= ½ Vmax * Line 7: Line 7: The units of Km are M, [[Concentration|concentration]]. The units of Km are M, [[Concentration|concentration]]. − Km indicates the [[Javascript:void(0);/*1512127072657*/|affinity]] of the enzyme for its substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]].
+ Km indicates the affinity of the enzyme for its substrate and thus the stability of the [[Enzyme-Substrate Complex|Enzyme-Substrate Complex]]. − Velocity is related to Kthrough the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S]).
+ Velocity is related to Km through the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S]). − *[[Vmax|Vmax]] = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration. + [[Vmax|Vmax]] = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration. − [S] = [[Substrate|substrate]] concentration.
+ [S] = [[Substrate|substrate]] concentration. − A reaction with a low Michaelis constant value indicates a low binding affinity, where as a large value indicates a high binding affinity.  + A reaction with a low Michaelis constant value indicates a low binding affinity, whereas a large value indicates a high binding affinityMichaelis, L; Menten, ML; Johnson, KA; Goody, R S. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper, + Biochemistry, 04 October 2011, Vol.50(39), pp.8264-9. −
+ === References
=== − = References  = + − + − Michaelis, L ; Menten, M L ; Johnson, K A ; Goody, R S. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper,
''Biochemistry,'' 04 October 2011, Vol.50(39), pp.8264-9 +

Latest revision as of 17:51, 6 December 2018

Michaelis constant is the substrate concentration at which the reaction velocity is equal to half the maximal velocity of the reaction.

Km = Michaelis constant

Km = the value of substrate concentration[S] that causes V= ½ Vmax *

The units of Km are M, concentration.

Km indicates the affinity of the enzyme for its substrate and thus the stability of the Enzyme-Substrate Complex.

Velocity is related to Km through the Michaelis & Menten equation: v = (Vmax [S])/(Km + [S]).

Vmax = maximum rate of reaction achievable for the enzyme under given conditions, only occurs at infinite substrate concentration.

[S] = substrate concentration.

A reaction with a low Michaelis constant value indicates a low binding affinity, whereas a large value indicates a high binding affinity.