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Bio Eng > Enzyme (Quiz 1) > Flashcards

Enzyme (Quiz 1) Flashcards

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Biology 101 flashcards
1
Q

are proteins that are catalysts of biochemical
reactions.
* Typically has a globular shape
* Complex 3-D structure

A

Enzyme

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2
Q

____ they are Biological Catalysts

  • Increase the rate of reaction by ____ of activation.
  • Catalyze nearly ____ the chemical reactions taking place in the cells of the body.
  • Have unique three-dimensional shapes that fit the shapes of ____.
A
  • Enzyme
  • lowering the energy of activation
  • all
  • reactants
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3
Q

net energy released from splitting of lactose

A

activation energy without enzyme

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4
Q

when chemical rxn’s activation energy decreased, net energy released

A

activation energy with enzyme

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5
Q

in 1833 the first clear recognition of enzyme was made by these two people

A

Payen and Persoz

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6
Q

an alcohol precipitate of malt extract contained in a thermolabile substance that converted strach into sugar.

A

diastase

Common name: alpha-amylase (a-amylase)

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7
Q

he was the first to crystallize enzyme

A

J.B. Sumner (1924-1930)

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8
Q

there are more than ____ biochemically important enzyme catalyzed reactions

A

2500

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9
Q

they are characterized by specificity for substrates

A

enzyme

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10
Q

they modulates an enzymes activity

A

effectors

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11
Q

enumerate the different types of effectors

A

Activators, inhibitors, both, or depending on conditions

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12
Q

its size could vary from small single unit to large multiple units

A

enzyme

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13
Q
  • Found in animal and plant cells
  • Needed to speed up the breakdown of HYDROGEN PEROXIDE
  • Breaks it down to OXYGEN and WATER
A

catalase

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14
Q
  • Found in saliva and in the pancreas
  • Break down enzyme
  • Breaks STARCH down to MALTOSE
A

amylase

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15
Q

Synthesis enzyme (builds up)
* Builds Glucose-1-Phosphate molecules into Starch
* The formation of starch is tested using iodine solution

A

Potato Phosphorylase

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16
Q

reaction of enzyme without substrate

A

no reaction

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17
Q

enzyme + substrate

Reaction?

A

rxn: water + oxygen (bubbles)

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18
Q

liver homogenation

A

catalase enzyme

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19
Q

– high efficiency, 10³ to 10¹⁷ faster than the corresponding uncatalyzed reactions.

A

Catalytic Efficiency

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20
Q

high specificity, interacting with one or a few specific substrates and catalyzing only one type of chemical reaction.

A

specificity

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21
Q

what are the mild reaction conditions?

A
  • 37°C,
  • physiological pH,
  • ambient atmospheric pressure.
22
Q

part of the enzyme where the reactants bind, and where the biochemical reaction occurs

A

active site

23
Q
  • Amino acid side chains interact, metal ions,
  • Various types of polar, non-polar, ionic interactions
A

enzyme active site

24
Q
  • The ____ is a region within an enzyme that fits the shape of molecules called _____
A

active site
substrate

25
Q
  • ____contains amino acid ____ that align and bind the ____.
  • and it Releases products when the _____ is complete
A
  • active site
  • R group
  • substrate
  • reaction is complete
26
Q

the substrate fit like a key in a lock, the active site is like a lock.

A

lock and key model

27
Q

they are small nonprotein molecules (cofactors and prosthetic group)

A

subunits

28
Q

apoenzyme + nonprotein part

A

holoenzyme

29
Q

what are the two chemical composition of enzyme

A

(1) Single Protein
(2) Conjugated Protein

30
Q

what are the two types of cofactor

A

coenzyme and prosthetic group

31
Q

the protein portion, inactive part of holoenzyme

A

apoenzyme

32
Q

it is the nonprotein portion, activator part of holoenzyme

A

cofactor

33
Q

they are loosely bound to enzyme (non-covalently bound)

A

coenzyme

34
Q

they are very tightly or even covalently bound to enzyme (covalently bound)

A

prosthetic group

35
Q

forms of active enzyme with only protein

A

simple enzyme

36
Q

forms of active enzymes that is formed by..

  • protein and metal ion
  • protein and organic molecule (coenzyme)
A

Enzyme + cofactor

37
Q

An additional non-protein molecule that is needed by some enzymes to help the reaction

A

cofactors

38
Q

are tightly bound cofactors

A

prosthetic groups

39
Q
  • Cofactors that are bound and released easily are called ____
  • Many vitamins are ___
A

coenzymes

40
Q
  • Many active enzymes require a __ as cofactors
  • Zn2+ cofactor for ___, stabilizes the ___ during the _____ of a peptide bond.
A
  • Metal Ions
  • carboxypeptidase
  • carbonyl oxygen
  • hydrolysis
41
Q
  • ___ catalyze the same reaction in different tissues in the body.
  • ________ , which converts lactate to ___, (LDH) consists of ____ .
A
  • isoenzymes
  • lactate dehydrogenase
  • pyruvate
  • five (5) isoenzymes
42
Q

Classification of Enzyme

  • IUPAC
  • EC
  • Four integer EC number and a name
  • Common name: usually the principal specific reactant + ___ (suffix)
  • Does not follow any rule (in naming)
    o ___
    o ___
A
  • -ase
  • pepsin
  • rhodanese
43
Q

Naming Enzyme

  • The name of an enzyme identifies the ____ substance, usually ends with -ase (sucrase from sucrose)
  • The name also describes the ____ of the enzyme (oxidases)
  • Sometimes common names are used, particularly for the ____ enzymes such as pepsin and trypsin
  • Some names describe both the ___ and the ___. (alcohol dehydrogenase oxides ethanol)
A
  • reacting substance
  • function of the enzyme
  • digestion enzymes
  • substrate and function
44
Q
  • catalyze oxidation-reduction reactions
  • used to convert L-Lactate (1 C bonded to O2) to Pyruvate (2 C bonded to O2) through Lactate dehydrogenase
A

oxidoreductases (dehydrogenases)

45
Q
  • catalyze group-transfer reaction, transfer groups of atoms
  • transferred amino group through alanine transaminase
A

transferases

46
Q
  • catalyze hydrolysis
  • used to convert pyrophosphate to phosphate (mechanism: water did chemistry to break a bond )
A

hydrolases

47
Q
  • addition/removal of a group to a double bonds without hydrolysis or oxidation
  • catalyze lysis of a substrate
A

lyases

48
Q
  • catalyze structural change within a single molecule
  • rearrangement of atoms
A

isomerases

49
Q

___ catalyze ligation or ____ of two substrates, use ____ to combine molecules

A
  • ligases
  • joining
  • ATP (Adenosine triphosphate)
50
Q

Enzymes are classified according to the type of reaction they catalyze

A

classification of enzyme

51
Q

Naming enzyme examples

  • _____ catalyzes the hydrolysis of sucrose
  • _____ catalyze oxidation reaction
A
  • sucrase
  • oxidases
52
Q

He initiated the use of -ase in naming enzyme

A

Duclaux (1898)

Bio Eng (6 decks)

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