ENZYMES Flashcards
enzymes that remove the elements of hydrogen, H2 or H− plus H+
Dehydrogenases
enzymes that hydrolyze proteins
Proteases
enzymes that catalyze rearrangements in configuration
Isomerases
enzymes that catayze oxidations and reductions
Oxidoreductases
enzymes that catayze transfer of moieties such as glycosyl, methyl, or phosphoryl groups
Transferases
Enzymes that catalyze hydrolytic cleavage of C—C, C—O, C—N, and other covalent bonds
Hydrolases
Enzymes that catalyze cleavage of C—C, C—O, C—N, and other covalent bonds by atom elimination, generating Double bonds
Lyases
enzymes that catalyze geometric or structural changes within a molecule
Isomerases
Enzymes that catalyze the joining together (ligation)of two molecules in reactions coupled to the hydrolysis of ATP
Ligases
are tighty an staby incorporate into a
protein’s structure by covaent bons or noncovaent forces.
Prosthetic Groups
serve functions simiar to those of prosthetic groups an overap with them. They bind weakly an transiently to their cognate enzymes or substrates, forming dissociabe compexes.
Cofactors
serve as recycabe shuttes that transport many substrates from one point within the cell to another.
Coenzymes
refers to reactions for which the ony participating acids or bases are protons or hydroxide ions
Specific Acid-Base Catalysis
Reactions whose rates are responsive to all the acis or bases present
general acid catalysis/ general base catalysis.
In orer to chemicay interact, substrate moecues must come
within bon-forming istance of one another. The higher
their concentration, the more frequenty they wi encounter
one another, an the greater wi be the rate at which reaction
proucts appear. When an enzyme bins substrate moecues
at its active site, it creates a region of high oca substrate concentration, one in which they are oriented in an ideal position
to chemically interact.
CATALYSIS BY PROXIMITY