The simplest way to investigate reaction rate is to monitor increase decrease( increase, decrease ) in reaction product against time. This can be done at a variety of substrate enzyme( substrate, enzyme ) concentrations and the initial velocity of the reaction determined. Eventually the reaction will reach a plateau when the reaction equilibrium has been attained.
In reality enzyme kinetics is more readily understood if we only consider the forward backwards( forward, backwards ) reaction and we define V0 as the number of moles grams litres( moles, grams, litres ) of product formed per second when the reaction is just beginning at t ~0

The higher lower( higher, lower ) the kcat and the lower the higher( the lower, the higher ) the KM the bigger the specificity constant.
The best substrate for an enzyme will have the highest lowest( highest, lowest ) specificity constant.
This constant also describe the catalytic catabolic( catalytic, catabolic ) efficiency of enzymes.

Inhibitors can also be very useful substances used as pharmaceuticals. Examples would be penicillin aspirin (methyl salicylate)( penicillin, aspirin (methyl salicylate) ) which inhibits the enzyme responsible for cell wall biosynthesis in certain bacteria and aspirin (methyl salicylate) and penicillin( and aspirin (methyl salicylate), and penicillin ) which binds to and inhibits cyclooxygenase enzymes.

There are two types of inhibition, REVERSIBLE and IRREVERSIBLE.
Reversible inhibition is said to be COMPETITIVE NON-COMPETITIVE OR UNCOMPETITIVE( COMPETITIVE, NON-COMPETITIVE OR UNCOMPETITIVE ) whereas irreversible inhibition can be NON-COMPETITIVE OR UNCOMPETITIVE. can be COMPETITIVE( can be NON-COMPETITIVE OR UNCOMPETITIVE., can be COMPETITIVE )

In competitive inhibition KM is increased decreased( increased, decreased ) but Vmax remains unaltered.
An example of competitive inhibition is inhibition of succinate dehydrogenase by malonate. Malonate competes with succinate for binding inhibition( binding, inhibition ) at the active site but cannot be converted to fumerate. Increasing Decreasing( Increasing, Decreasing ) the concentration of succinate competes out the inhibitor.

In uncompetitive inhibition KM is unaltered or appears reduced increased( unaltered or appears reduced, increased ) and Vmax is dramatically reduced increased( dramatically reduced, increased )
There is no requirement for the inhibitor to resemble the structure of the substrate enzyme( substrate, enzyme ). The inhibitor does not bind to free enzyme only to ES complexed S( ES complexed, S ) enzyme. It is believed that these type of inhibitors distort the active site region preventing inducing( preventing, inducing ) further substrate turnover.

A non-competitive inhibitor binds to both the free E and the ES complex and the effect of this is to lower increase( lower, increase ) the effective number of enzyme molecules. The rsult is a decrease an increase( a decrease, an increase ) in Vmax as a result of changes in kcat Km Vo Kd( kcat, Km, Vo, Kd ).
Vmax is reduced increased( reduced, increased ) and KM is not normally effected