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47 Cards in this Set

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oxidize or reduce substrates
Oxidoreductases
transfer a functional group from one molecule to another
Transferases
cleave bonds with water
Hydrolases
remove a group to form a double bond or add of a group to a double bond
Lyases
catalyze intermolecular rearrangements
Isomerases
catalyze the joining of two molecules
Ligases
electron donator
reductant
electron acceptor
oxidant
utilize one atom of oxygen from O2 as electron acceptor
Monooxygenases
incorporate both atoms of O2 into a substrate as electron acceptor
Dioxygenases
uses nucleotide triphosphate to transfer phosphate to small molecule or protein
Kinase
utilizes acetyl CoA to transfer acetyl group to acceptor
Acyltransferase
interconverts amino and keto acids by transferring an amino group between them
Aminotransferase
catalyze hydrolysis reactions
Hydrolases
is the addition of water to a chemical bond in an essentially irreversible reaction
Hydrolysis
Hydrolysis of cholesterol ester produces ??
cholesterol (an alcohol) and fatty acid
are enzymes that hydrolyze the phospho–ester bond
RNase and DNase
usually cleave carbon–carbon bonds, although other enzymes form or break a carbon–nitrogen bonds or release a CO2 from a β-keto acid.
Lyases
Some lyases require ?? as the cofactor
pyridoxal phosphate
?? does not require nucleotide triphosphate for the reaction, unlike synthetases
Synthase
moves phosphate within the same molecule
Mutase
These may change the stereochemistry at a carbon atom
Isomerases and epimerases
require energy to join carbon atoms together
Ligases
is a reagent that forms a chemical bond to its reaction partner by donating both bonding electrons; Lewis Base; usually a negative ion
nucleophile
is a reagent attracted to electrons that participates in a chemical reaction by accepting an electron pair in order to bond; Lewis Acid; usually a positive ion
electrophile
ability to donate protons (H+) to another compound; accept a pair of electrons
Acid
ability to accept protons (H+) to another compound; donates a pair of electrons
Base
Involved in oxidation–reduction reactions catalyzed by dehydrogenases
Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP)
Dehydrogenase that is more often involved in catabolism
NAD-dependent dehydrogenases
Dehydrogenase that is usually involved in anabolism
NADP-dependent dehydrogenases
is similar structural motif binding NAD(P) in most dehydrogenases
Rossmann fold
has phosphate esterified to ribitol
Flavin mononucleotide (FMN)
is Flavin mononucleotide with adenosine linked by pyrophosphate to riboflavin
Flavin adenine dinucleotide (FAD)
primarily involved in reactions involving amino acids
Pyridoxal phosphate
introduces an amino group into a compound.
Transamination
contain a tightly bound transition metal, e.g. Zn2+ or Fe2+
Metalloenzymes
Cross-links form via the action of ???, which oxidatively deaminates the amino groups of certain lysines and hydroxylysine residues, yielding reactive aldehydes which react and form cross-links
lysyl oxidase
Donors–acceptor pairs
saturated carbon-carbon bonds-?
Donors–acceptor pairs
unsaturated
Donors–acceptor pairs
alcohols-??
aldehydes
Donors–acceptor pairs
aldehydes-??
acids
Donors–acceptor pairs
amines–??
imines
Forms of niacin
NAD & NADP
Forms of riboflavin
FMN & FAD
Michaelis-Menten equation
Vmax[S] / Km + [S]
When n = ½ Vmax, Km = ??
concentration of substrate
What enables approximation of rates of enzymatic reactions by assuming [ES] concentration is constant; important in Michaelis constant
Steady-state assumption
Other common names for ligases include and uses ATP
synthetases