Enzymes Flashcards

1
Q

Complex organic compound which has the ability of speeding chemical reactions without being affected in the process.

A

Enzymes

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2
Q

study of enzymes

A

Enzymology

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3
Q

Enzymes functions as being _______ (catalyze on reactions in living systems.)

A

Biological Catalyst

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4
Q

Because enzymes are protein in nature, they are sensitive to any or all of denaturing agents including change in pH of the medium

A

true

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5
Q

Enzymes work best at temperatures between ______

A

35-40 degrees Celsius

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6
Q

Enzymes are highly selected and follow the principle of ___________.

A

Lock and Key Theory

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7
Q

Enzymes contain ___ weight as Nitrogen

A

16%

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8
Q

the non-protein group in an enzyme

A

Prosthetic Group

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9
Q

the protein portion

A

Apoenzyme

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10
Q

two portions combined together in co-factors

A

Holoenzyme

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11
Q

non -protein organic compounds derived from vitamins

A

Co-enzyme

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12
Q

some cofactors are only transiently associated with a given enzyme molecule, so that they function as ______.

A

Cosubstrates

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13
Q

the non-enzyme part of the Co-enzyme is termed

A

Co-factor

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14
Q

are inactive form of enzymes. eg: pepsinogen

A

Zymogens or Proenzymes

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15
Q

FAD

A

Flavine Adenine Dinucleotide

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16
Q

NAD

A

Nicotinamide Adenine Dinucleotide

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17
Q

FMN

A

Flavine Mononucleotide

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18
Q

involved in carbon dioxide fixation reactions and fatty acid synthesis

A

Biotin

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19
Q

coenzyme involved in the transfer of methyl groups;
active in amino acid metabolism

A

Vitamin B12 (cyanocobalamin)

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20
Q

needed for cellular and macrocellular syntheses

A

Vitamin E

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21
Q

Coenzyme used in electron transport (naphthaquinones and quinones)

A

Vitamin K

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22
Q

The 2 Co-factors

A

Co-enzyme
Metal-ion Activator

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23
Q

are the inorganic ions of the co-factors

A

Metal-ion Activator

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24
Q

contains an apoenzyme and metal ion cofactor

A

Metalloenzyme

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25
Q

Vitamin B2

A

Riboflavin

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26
Q

Vitamin B1

A

Thiamine

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27
Q

Vitamin B 12

A

Cobalamin

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28
Q

ascorbic acid

A

Vitamin C

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29
Q

Vitamin B6

A

Pyridoxine

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30
Q

the region of the enzyme that binds the substrate to form enzyme-substrate complex.

A

Active Site

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31
Q

6 major classifications of Enzymes

A

Hydrolases
Oxidoreductases
Transferases
Lyases
Isomerases
Ligases

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32
Q

are also known as synthetase

A

Ligase

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33
Q

are ATP dependent enzymes catalyzing biosynthetic reactions

A

Synthetases

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34
Q

are enzymes catalyzing biosynthesis reaction but do not require ATP

A

Synthases

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35
Q

Class of Enzymes According to CHEMICAL REACTION CATALYZED

A

Addition of Water Molecules
Transfer of Electrons
Splitting/Forming a C-C Bond
Transfer of a Radical

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36
Q

Addition of Water Molecules / Hydrolase:

A

Carbohydrase
Esterases
Nucleases
Amidases
Proteases
Peptidases

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37
Q

aid in the hydrolysis of carbohydrates

A

Carbohydrase

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38
Q

under Carbohydrase: BALMS

A

beta amylase (starch & glycogen to dextrin & maltose)
alpha amylase (starch & glycogen to dextrin)
lactase (lactose to glucose & galactose)
maltase (maltose to glucose)
sucrase (sucrose to glucose & fructose)

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39
Q

aid in the hydrolysis of esters

A

Esterases

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40
Q

under Esterases: (LPC)

A

Lipases (glycerides to fatty acids & glycerol)
Phosphatase (organic phosphates to phosphoric acid)
Choline Esterase/Cholinesterase (acetyl choline to acetic acid & choline)

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41
Q

aid in the hydrolysis of nucleic acids

A

Nucleases

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42
Q

under Nucleases:

A

Polynucleotidases (nucleic acid to nucleotides)
Nucleotidases (nucleotides to nucleosides & phosphoric acid)
Nucleosidase (nucleosides to sugar and purine)

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43
Q

aide in the hydrolysis of amides

A

Amidases

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44
Q

under amidases: (UA)

A

Ureases (urea to ammonia & CO2)
Arginase (arginine to ornithine & urea)

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45
Q

aid in the hydrolysis of protein

A

Proteases

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46
Q

under proteases:

A

Pepsin (proteins to proteoses & peptones)
Rennin (casein to paracasein)
Trypsin (cleaves the polypeptide chain from carboxyl end of arg and lys)
Chymotrypsin (cleaves the polypeptide chain from carboxyl end of Phe, Trp, Tyr)
Cathepsin (proteins to proteoses & peptones)
Bromelin/Bromelain (proteins to proteoses & peptones)

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47
Q

hydrolyze peptides to simple peptides and amino acids

A

Peptidases

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48
Q

under peptidases: (PCAD)

A

Prolinase (polypeptides containing praline to simpler peptides and praline)
Carboxypolypeptidases (sequentially cleave polypeptide chain from carboxyl term.)
Aminopolypeptidases (sequentially cleave polypeptide chain from amino term.)
Dipeptidases (dipeptides to amino acids)

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49
Q

are enzymes which catalyze the removal of hydrogen from a substrate and pass it directly to oxygen

A

Oxidases

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50
Q

Examples of OXIDASES (DCAPT)

A

Dehydrogenases (activates H atoms of organic compounds)
Catalase (acts on Hydrogen Peroxide to give water & Oxygen)
Peroxidases (act on organic peroxides giving nascent oxygen)
Ascorbic Acid Oxidase (acts on ascorbic Acid)
Tyrosinase (acts on tyrosine)

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51
Q

catalyze the linkage not broken by water; splitting or forming a C-C bond

A

Desmolases

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52
Q

under Desmolases: (DCC)

A

Decarboxylases
- Carboxylase (alpha keto acids to CO2 & aldehydes)
- Carbonic & Anhydrase (carbonic acid to water & CO2)

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53
Q

catalyze the transfer of amino groups from amino acids to ketoacids and promotes the formation of new amino acids.

A

Transaminases

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54
Q

under transaminase: (AG)

A

Alanine Transaminase
Glutamate Transaminase

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55
Q

catalyzes transfer of alpha-amino group from amino acid to pyruvic acid to produce alpha keto acid and alanine

A

Alanine Transaminase

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56
Q

catalyzes transfer of alpha-amino group from amino acid to alpha-ketoglutyaric acid to produce alpha keto & glutamic acid

A

Glutamate Transaminase

57
Q

all Enzymes are protein EXCEPT

A

Ribozymes / RNA molecules

58
Q

Enzymes can work /cooperate with non-protein portion called ____?

A

Co-factors

59
Q

co-factors remain tightly bound to an enzyme
most are metals

A

metal ion activator (prosthetic group)

60
Q

molecules that enter enzymatic reactions
substances which the enzymes act

A

Substrates

61
Q

non-protein , required for enzymatic activities
organic / inorganic

A

Co-factors

62
Q

protein without bound cofactor
aka. APOPROTEIN

A

APOENZYME

63
Q

active form of enzyme
coenzyme (organic) + apoenzyme
metal ion activator (inorganic) + apoenzyme

A

Holoenzyme

64
Q

contains apoenzyme and a metal ion co-factor

A

metalloenzyme

65
Q

organic compounds derived from vitamins

A

coenzymes

66
Q

FAD (FLAVINE ADENINE DINUCLEOTIDE)

A

VITAMIN B2 (RIBOFLAVIN)

67
Q

NAD (NICOTINAMIDE ADENINE DINUCLEOTIDE)

A

NIACINE - VITAMIN B3
COMMONLY FOUND IN VITAMINS

68
Q

PROTEOLYTIC ENZYMES

A

PEPSIN
ALCALASE
BROMELAINS
PAPAIN
TRYPSIN
SUTILAINS
RENNIN
EREPSIN
STREPTOKINASE
UROKINASE
FIBRINOLYSIN

69
Q

from Sus scrofa, fam suidae
assist in gastric digestion
found in gastric juice
PROTEINS to PROTEASES & PEPTONES
digestive aid of pre-cooked foods

A

PEPSIN

70
Q

additive to remove protein stains

A

ALCALASE

71
Q

mix of protein-digesting & milk clotting enzymes from Ananas comosus, Fam Bromeliaceae
meat tenderizer
therapy to reduce inflammation & edema
accelerate tissue repair, esp. following episiotomy

A

BROMELAINS

72
Q

from latex of Carica Papaya, Caricaceae
relieve symptoms of episiotomy - clean Contact Lenses
meat/Beef tenderizer
SKIN WHITENER
stabilizer for chill proof beer

A

PAPAIN

73
Q

nonpyrogenic proteolytic enzyme
relieves lower back pain

A

CHYMOPAPAIN

74
Q

PROTEASES to POLYPEPTIDES & AMINO ACIDS
by pancreas
for wound debridement

A

TRYPSIN

75
Q

from extract of pancreatic gland of Ox
for ophthalmic solution

A

CHYMOTRYPSIN

76
Q

from bacillus subtilis
for wound debridement

A

SUTILAINS

77
Q

coagulated enzyme present in mucous membrane of animal stomach
soluble cassein milk
for cheesemaking

A

RENNIN

78
Q

intestinal juice
PROTEOSES & PEPTONES to AMINO ACIDS

A

EREPSIN

79
Q

purified bacterial protein by group C B-hemolytic streptococci
as lyophilized powder
PLASMINOGEN to PLASMIN

A

STREPTOKINASE

80
Q

human urine or from human kidney cells
PLASMINOGEN to PLASMIN

A

UROKINASE

81
Q

in blood serum as a protease, profibrinolysin or plasminogen
activate human blood plasma fraction with streptokinase

A

FIBRINOLYSIN

82
Q

formation of blood clot

A

THROMBOSIS

83
Q

OXIDIZING ENZYMES (PerTh)

A

PEROXIDASE
THROMBIN

84
Q

PLANTS!
oxidation reactions cause discoloration of bruised fruits

A

PEROXIDASE

85
Q

fibrinogen of circulating blood into insoluble fibrin
COAGULATION FACTOR II

A

THROMBIN

86
Q

CARBOHYDRASE / AMYLOLYTIC ENZYMES

A

AMYLASE
DIASTASE
AMYLOPSIN
INVERTASE / SUCRASE
ZYMASE
EMULSIN
MYROSIN
AMYLOGLUCOSIDASE
CELLULASE
LACTASE
PECTINASE
HYALURONIDASE

87
Q

in salivary glands
aka. salivary diastase / ptyalin

A

AMYLASE

88
Q

yellowing white, malt
POTATO to SUGAR

A

DIASTASE

89
Q

digestive tract of animals
aka. animal diastase

A

AMYLOPSIN

90
Q

yeast and intestinal juice
SUCROSE to GLUCOSE & FRUCTOSE
CANDIES!!

A

INVERTASE / SUCRASE

91
Q

MONOSACCHARIDES to ALCOHOL & CO2

A

ZYMASE

92
Q

ALMONDS!!

A

EMULSIN

93
Q

white and black mustard

A

MYROSIN

94
Q

dextrose from starch

A

AMYLOGLUCOSIDASE

95
Q

COFFEE

A

CELLULASE

96
Q

lactose crystals ICE CREAM

A

LACTASE

97
Q

WINES & JUICES

A

PECTINASE

98
Q

HYALURONIC ACIDS
SPREADING DIFFUSING FACTOR AGENT
HUMAN TESTES/ LOEECHES/SNEK VENOMS

A

HYALURONIDASE

99
Q

ESTERASES - LUPS

A

LIPASE
UREASE
PECTASE
STEAPSIN

100
Q

lipolytic enzyme, animal and veggie kingdom
]pancreatic juice of animals
cheese flavor production

A

LIPASE

101
Q

PECTIN to PECTIDE ACID & METHYL ALCOHOL

A

PECTASE

102
Q

lipolytic enzyme, digesting dietary fat

A

STEAPSIN

103
Q

UREA to AMMONIA
SOYBEANS!!!!

A

UREASE

104
Q

OTHERS???? - CoL-ALip

A

COLLAGENASE
L-ASPARAGINASE
LIPOXYGENASE

105
Q

clostridium histolyticum
cleaves collagen for ulcers and burns

A

COLLAGENASE

106
Q

FROM ESCHERICHIA COLI (E. COLI)
for leukemia

A

L-ASPARAGINASE

107
Q

BREAD - WHITENING

A

LIPOXYGENASE

108
Q

temporary intermediate compound forms

A

enzyme - substrate complex

109
Q

min. amount of energy that is required to activate atoms or molecules to a condition in which they can undergo chemical transformation or physical transport

A

ACTIVATION ENERGY

110
Q

theories explaining mode of enzyme action

A

FISCHER’S LOCK AND KEY THEORY
KOSHLAND’S INDUCED FIT THEORY

111
Q

ENZYME - SUBSTRATE (F-5) COMPLEX THEORY
the active site of the enzyme and substrate have complementary structures, hence they fit together as a key fits a lock.

A

FISCHER’S LOCK AND KEY THEORY

112
Q

in this model, some type of modification is induced in the substrate, enzyme, or both.
modification begins process of reaction.

A

KOSHLAND’S INDUCED FIT THEORY

113
Q

FACTORS THAT INFLUENCE ENZYME ACTION

A

Concentration of Substrates
Concentration of Enzymes
Temperature
pH
Presence of Accelerators
Presence of Inhibitors
Environmental Hazards

114
Q

the optimum temperature of enzyme in the body

A

37 degrees Celsius

115
Q

they activate the enzyme

A

accelerators

116
Q

have the ability to combine with enzyme in a reversible and irreversible reaction and hence block enzyme catalysis

A

Inhibitors

117
Q

environmental hazards

A

Hg (mercury) - phenyl mercuric acetate & methyl mercuric acetate
Cd (cadmium) - cigarette smoke
Pb (lead) - gasoline / yellow-painted pencils

118
Q

in CLINICAL ENZYMOLOGY, Enzymes are commonly used in medicine as:

A

Analytical tools or reagents for measuring quantities
As index for pathology of diseases

119
Q

in acute pancreatitis, perforated duodenal and peptic ulcers and intestinal obstruction

A

LIPASE

120
Q

in blood after MI
sensitive indicator in the early stages of myocardial ischemia

A

Creatine Phosphokinase (CPK)

121
Q

found in skeletal and heart muscle

A

MM(CK3)

122
Q

found in heart muscles

A

MM(CK2)

123
Q

found in brain

A

BB(CK1)

124
Q

in rickets, obstructive jaundice

A

Alkaline Phosphatase

125
Q

carcinoma of prostate (prostate cancer)

A

Acid Phosphatase

126
Q

viral heap, heart and skeletal muscle disease

A

LDH - Lactase Dehydrogenase

127
Q

in Myocardial infarction

A

AST - Aspartate Transaminase

128
Q

in liver disease

A

ALT - Alanine Transaminase

129
Q

in liver disease, biliary obstruction (gallstone)

A

Glutamyl Transferase

130
Q

moderately increase in hepatitis and highly elevated biliary obstruction

A

5’ Nucleotidase

131
Q

use as treatment of pulmonary embolism, coronary artery thrombosis and restoring the patency of intravenous catheters

A

Urokinase

132
Q

use as treatment of pulmonary embolism, deep vein thrombosis, arterial thrombosis and embolism, arteriovenous cannula acclusion and coronary artery thrombosis

A

Streptokinase

133
Q

use as treatment of blood clots within the cardiovascular system, exclusive of thrombi of the coronary and cerebral arteries

A

Fibrinolysin

134
Q

the prosthetic group; makes the enzyme active, “active site”

A

Conjugated protein

135
Q

used for adjunctive therapy to reduce inflammation and edema
accelerate tissue repair, esp. following episiotomy

A

Bromelains

136
Q

enzymes used for testing Triglycerides

A

Lipase

137
Q

enzyme used to test polymerase chain reaction

A

Reverse Transcriptase

138
Q

The 3 CK isoenzymes:

A

MM(CK3)
MM(CK2)
BB(CK1)