← Discover
Biochemistry
Enzymes and Reaction Rates
12 terms · by ineedtostudy · updated 4 hours ago
Sign up or log in to track what you have mastered. You can still study this set as a guest.
Flashcards
Flip through the deck and sort each card into “still learning” or “got it”.
Learn
Adaptive rounds — multiple choice first, then typing, weakest cards more often.
Match
Race the clock pairing terms with definitions. Six pairs a round.
Test
A graded mock exam: written, multiple choice and true/false, marked at the end.
Crossword
Terms become answers, definitions become clues. Solve it here or print it.
Terms in this set
Enzyme
A biological catalyst that lowers activation energy without being consumed or changing the equilibrium position.
Active site
The pocket where substrate binds and catalysis happens.
Induced fit
The active site changes shape slightly on binding to grip the substrate — the refinement of the older lock-and-key model.
Substrate
The molecule an enzyme acts on.
Competitive inhibitor
Binds the active site and competes with substrate. Raises apparent Km; Vmax is unchanged.
Non-competitive inhibitor
Binds elsewhere and changes the enzyme's shape. Lowers Vmax; Km is unchanged.
Km
The substrate concentration at half-maximal velocity. A low Km means high affinity.
Vmax
The maximum rate, reached when every active site is saturated with substrate.
Cofactor
A non-protein helper an enzyme needs — often a metal ion such as Zn2+ or Mg2+.
Coenzyme
An organic cofactor, frequently vitamin-derived: NAD+, FAD, coenzyme A.
Allosteric regulation
Binding at a site away from the active site turns activity up or down.
Denaturation
Loss of three-dimensional structure from heat or pH, destroying activity. The sequence is unchanged.