Enzymes

They’re : faster, work in milder conditions, have greater specificity, and the potential to be regulated.

inverse and exponential

Substrate specificity and catalytic power

Reducing entropy, desolvation of the substrate to expose reactive groups, alignment of reactive functional groups of the enzyme with the substrate, distortion of substrates, induced fit of the enzyme in response to substrate binding.

are stable compound whose structures resemble unstable transition states

maximum velocity of the enzyme

is [S] required to reach 1/2 Vman

Vmax[S]/Km + [S]

a compound that binds to an enzyme to interfere with its activity.

formation of ES, the breakdown to E and P

bind to the enzyme by non-covalent interactions

form stable covalent bonds with the enzyme to inactivate the enzyme

are initially unreactive but are converted to a reactive species that inactivates the enzyme. Also called Biochemical trojan horses or Mechanism-based inactivators

peptide bonds

pancreas (inactive zymogens)

selective proteolysis

Lys and Arg

Phe and Tyr

Gly and Ala

Long term-control amount of the enzyme that is present, short-term adjusting the activity of a constant quantity of the enzyme

phosphorylation, methlation, glyosylation

allosteric regulation

phosphoryl goups

phosphoryl groups