Exam 1 - Enzymes

Front 1

oxidize or reduce substrates

Back 1

Oxidoreductases

Front 2

transfer a functional group from one molecule to another

Back 2

Transferases

Front 3

cleave bonds with water

Back 3

Hydrolases

Front 4

remove a group to form a double bond or add of a group to a double bond

Back 4

Lyases

Front 5

catalyze intermolecular rearrangements

Back 5

Isomerases

Front 6

catalyze the joining of two molecules

Back 6

Ligases

Front 7

electron donator

Back 7

reductant

Front 8

electron acceptor

Back 8

oxidant

Front 9

utilize one atom of oxygen from O2 as electron acceptor

Back 9

Monooxygenases

Front 10

incorporate both atoms of O2 into a substrate as electron acceptor

Back 10

Dioxygenases

Front 11

uses nucleotide triphosphate to transfer phosphate to small molecule or protein

Back 11

Kinase

Front 12

utilizes acetyl CoA to transfer acetyl group to acceptor

Back 12

Acyltransferase

Front 13

interconverts amino and keto acids by transferring an amino group between them

Back 13

Aminotransferase

Front 14

catalyze hydrolysis reactions

Back 14

Hydrolases

Front 15

is the addition of water to a chemical bond in an essentially irreversible reaction

Back 15

Hydrolysis

Front 16

Hydrolysis of cholesterol ester produces ??

Back 16

cholesterol (an alcohol) and fatty acid

Front 17

are enzymes that hydrolyze the phospho–ester bond

Back 17

RNase and DNase

Front 18

usually cleave carbon–carbon bonds, although other enzymes form or break a carbon–nitrogen bonds or release a CO2 from a β-keto acid.

Back 18

Lyases

Front 19

Some lyases require ?? as the cofactor

Back 19

pyridoxal phosphate

Front 20

?? does not require nucleotide triphosphate for the reaction, unlike synthetases

Back 20

Synthase

Front 21

moves phosphate within the same molecule

Back 21

Mutase

Front 22

These may change the stereochemistry at a carbon atom

Back 22

Isomerases and epimerases

Front 23

require energy to join carbon atoms together

Back 23

Ligases

Front 24

is a reagent that forms a chemical bond to its reaction partner by donating both bonding electrons; Lewis Base; usually a negative ion

Back 24

nucleophile

Front 25

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

Back 25

electrophile

Front 26

ability to donate protons (H+) to another compound; accept a pair of electrons

Back 26

Acid

Front 27

ability to accept protons (H+) to another compound; donates a pair of electrons

Back 27

Base

Front 28

Involved in oxidation–reduction reactions catalyzed by dehydrogenases

Back 28

Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP)

Front 29

Dehydrogenase that is more often involved in catabolism

Back 29

NAD-dependent dehydrogenases

Front 30

Dehydrogenase that is usually involved in anabolism

Back 30

NADP-dependent dehydrogenases

Front 31

is similar structural motif binding NAD(P) in most dehydrogenases

Back 31

Rossmann fold

Front 32

has phosphate esterified to ribitol

Back 32

Flavin mononucleotide (FMN)

Front 33

is Flavin mononucleotide with adenosine linked by pyrophosphate to riboflavin

Back 33

Flavin adenine dinucleotide (FAD)

Front 34

primarily involved in reactions involving amino acids

Back 34

Pyridoxal phosphate

Front 35

introduces an amino group into a compound.

Back 35

Transamination

Front 36

contain a tightly bound transition metal, e.g. Zn2+ or Fe2+

Back 36

Metalloenzymes

Front 37

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

Back 37

lysyl oxidase

Front 38

Donors–acceptor pairs
saturated carbon-carbon bonds-?

Back 38

Donors–acceptor pairs
unsaturated

Front 39

Donors–acceptor pairs
alcohols-??

Back 39

aldehydes

Front 40

Donors–acceptor pairs
aldehydes-??

Back 40

acids

Front 41

Donors–acceptor pairs
amines–??

Back 41

imines

Front 42

Forms of niacin

Back 42

NAD & NADP

Front 43

Forms of riboflavin

Back 43

FMN & FAD

Front 44

Michaelis-Menten equation

Back 44

Vmax[S] / Km + [S]

Front 45

When n = ½ Vmax, Km = ??

Back 45

concentration of substrate

Front 46

What enables approximation of rates of enzymatic reactions by assuming [ES] concentration is constant; important in Michaelis constant

Back 46

Steady-state assumption

Front 47

Other common names for ligases include and uses ATP

Back 47

synthetases