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BIOCHEMISTRY > VITAMINS AND ENZYMES > Flashcards

VITAMINS AND ENZYMES Flashcards

1
Q

is an organic compound that acts as a catalyst for a biochemical reaction

A

Enzymes

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2
Q

is an enzyme composed only of protein (amino acid chains).

A

simple enzyme

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3
Q

is an enzyme that has a nonprotein part in addition to a protein part

A

conjugated enzyme

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4
Q

is the nonprotein part of a conjugated enzyme. It is the combination of apoenzyme with a cofactor that produces a biochemically active enzyme

A

cofactor

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5
Q

is the protein part of a conjugated enzyme.

A

apoenzyme

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6
Q

is the biochemically active conjugated enzyme produced from an apoenzyme and a cofactor.

A

holoenzyme

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7
Q

is a small organic molecule that serves as a cofactor in a conjugated enzyme.

A

coenzyme

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8
Q

is the reactant in an enzyme-catalyzed reaction

A

substrate

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9
Q

is an enzyme that catalyzes an oxidation–reduction reaction

A

oxidoreductase

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10
Q

is an enzyme that catalyzes the transfer of a functional group from one molecule to another.

A

A transferase

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11
Q

catalyzes the transfer of an amino group from one molecule
to another.

A

transaminase

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12
Q

catalyze the transfer of a phosphate group from adenosine triphosphate (ATP) to give adenosine diphosphate (ADP) and a phosphorylated product (a
product containing an additional phosphate group).

A

Kinases

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13
Q

is an enzyme that catalyzes a hydrolysis reaction in which the addition
of a water molecule to a bond causes the bond to break

A

hydrolase

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14
Q

effect the breaking of peptide linkages in proteins, and lipases effect the breaking of ester linkages in triacylglycerols

A

proteases

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15
Q

is an enzyme that catalyzes the addition of a group to a double bond or the
removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

A

lyase

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16
Q

effects the removal of the components of water from a double bond

A

dehydratase

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17
Q

is an enzyme that catalyzes the isomerization (rearrangement of atoms)
of a substrate in a reaction, converting it into a molecule isomeric with itself

A

isomerase

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17
Q

effects the addition of the components of water to a double bond.

A

hydratase

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18
Q

is an enzyme that catalyzes the bonding together of two molecules into one
with the participation of ATP

A

ligase

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19
Q

is the relatively small part of an enzyme’s structure that is actually involved in catalysis.

A

active site

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20
Q

is the intermediate reaction species that is formed when a substrate binds to the active site of an enzyme

A

enzyme–substrate complex

21
Q

the active site in the enzyme has a fixed, rigid geometrical conformation.

A

Lock-and-Key Model

22
Q

allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate

A

The induced-fi t model

23
Q

an enzyme will catalyze a particular
reaction for only one substrate

A

Absolute Specificity

24
Q

an enzyme can distinguish between
stereoisomers.

A

Stereochemical Specificity

25
Q

involves structurally similar compounds that have the same functional groups

A

Group Specificity

26
Q

involves a particular type of bond, irrespective of the structural features in the vicinity of the bond.

A

Linkage Specificity

27
Q

is a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction

A

Enzyme activity

28
Q

is the temperature at which an
enzyme exhibits maximum activity

A

Optimum temperature

29
Q

which is active in the stomach, functions best at a pH of 2.0

A

Pepsin

30
Q

which operates in the small intestine, functions best at a pH of 8.0

A

trypsin

31
Q

is the number of substrate molecules transformed per minute by one
molecule of enzyme under optimum conditions of temperature, pH, and saturation.

A

turnover number

32
Q

Reaction rate increases with
increasing enzyme
concentration, assuming
enzyme concentration is much
lower than that of substrate.

A

Concentration
of Enzyme

33
Q

is a substance that slows or stops the normal catalytic function of an enzyme by binding to it

A

enzyme inhibitor

34
Q

is a molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can
compete with the substrate for occupancy of the enzyme’s active site.

A

competitive enzyme inhibitor

35
Q

is a molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site

A

noncompetitive enzyme inhibitor

36
Q

is a molecule that inactivates enzymes by forming a strong covalent bond to an amino acid side-chain group at the enzyme’s active site

A

irreversible enzyme inhibitor

37
Q

A molecule closely resembling the
substrate. Binds to the active site and
temporarily prevents substrates from
occupying it, thus blocking the reaction

A

Competitive Enzyme Inhibitor

38
Q

A molecule that binds to a site on an
enzyme that is not the active site. The
normal substrate still occupies the active site but the enzyme cannot catalyze the reaction due to the presence of the Inhibitor

A

Noncompetitive Enzyme Inhibitor

39
Q

A molecule that forms a covalent bond to a part of the active site, permanently
preventing substrates from occupying it.

A

irreversible Enzyme Inhibitor

40
Q

is an enzyme with two or more protein chains (quaternary structure) and two kinds of binding sites (substrate and regulator

A

allosteric enzyme

41
Q

increases enzyme activity; the shape of the active site is changed such that it can more readily accept substrate

A

positive regulator

42
Q

(a noncompetitive inhibitor) decreases enzyme activity; changes to the active site are such that substrate is less readily accepted

A

negative regulator

43
Q

is a process in which activation or inhibition of the fi rst reaction in a
reaction sequence is controlled by a product of the reaction sequence.

A

Feedback control

44
Q

is an enzyme that catalyzes the breaking of peptide bonds that maintain the primary structure of a protein

A

proteolytic enzyme

45
Q

is the inactive precursor of a proteolytic enzyme.

A

A zymogen

46
Q

and the removal of the phosphate group from the enzyme is called

A

dephosphorylation

47
Q

The process of addition of the phosphate group to the enzyme is called

A

phosphorylation

47
Q

is a process in which enzyme activity is altered by covalently modifying the structure of the enzyme through attachment of a chemical group to or
removal of a chemical group from a particular amino acid within the enzyme’s structure.

A

Covalent modification

48
Q

is a substance that kills bacteria or inhibits their growth

A

antibiotic

49
Q
A
50
Q
A

BIOCHEMISTRY (8 decks)

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