1.
activation: enzyme catalyze biological reactions by lowering the ___ energy needed for the reaction to proceed
2.
active site: relatively small portion of an enzyme that is involved in substrate binding
3.
apoenzyme: hemoglobin without the heme, for example
4.
coenzyme: organic cofactor required for certain enzymes to be active
5.
cofactor: a molecule essential to the functioning of an enzyme but not part of the enzyme protein itself (divalent cation)
6.
competitive: type of inhibitor that alters the Km of an enzyme without altering Vmax
7.
covalent: regulation of enzyme activity by the reversible binding of a phosphoryl group is an example of regulation by ___ modification
8.
feedback: type of inhibition in which increasing concentrations of a reaction pathway's product decreases the activity of an allosteric enzyme eary in that pathway
9.
first order: ___reactions involve a single substrate molecule and the rate depends only on [S]
10.
ground state: energetic state of a substrate or product molecule in its most energetically stable form
11.
haloenzyme: complete enzyme complex including all the protein subunits and prosthetic groups
12.
induced fit: describes changes in the conformation of an enzyme upon substrate binding
13.
inhibitor: agent that reduces the overall rae of an enzyme-catalyzed reaction
14.
kinetics: the study of reaction rates in biological systems is referred to as enzyme ____
15.
michaelis menton: __kinetics describes the enzymatic activity of an idealized enzyme
16.
noncompetitive: a specific, rare type of mixed inhibitor that alters Vmax without affecting Km
17.
prosthetic: some enzymes have a covalently linked ____ group essential to its activity
18.
rate limiting: the slowest reaction in a sequence is the ___ step
19.
steady state: the assumption that the rate of formation of ES is exactly equal to the rate of breakdown of ES is called the ____ assumption
20.
substrate: molcule that binds to the active site of an enzyme
21.
transition: the top of the energy hill is the___ state
22.
transition state: a _____ analog binds more tightly to the active site than does the substrate molecule
23.
turnover: Kcat is known as the ____ number. At saturating substrate concentration Kcat = Vmax/[Et]
24.
zero: When the K'eq = one, /\G'° =
25.
zymogen: trypsin is to trypsinogen as active enzyme is to___
