Enzymes Flashcards
1
Q
Complex organic compound which has the ability of speeding chemical reactions without being affected in the process.
A
Enzymes
2
Q
study of enzymes
A
Enzymology
3
Q
Enzymes functions as being _______ (catalyze on reactions in living systems.)
A
Biological Catalyst
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
5
Q
Enzymes work best at temperatures between ______
A
35-40 degrees Celsius
6
Q
Enzymes are highly selected and follow the principle of ___________.
A
Lock and Key Theory
7
Q
Enzymes contain ___ weight as Nitrogen
A
16%
8
Q
the non-protein group in an enzyme
A
Prosthetic Group
9
Q
the protein portion
A
Apoenzyme
10
Q
two portions combined together in co-factors
A
Holoenzyme
11
Q
non -protein organic compounds derived from vitamins
A
Co-enzyme
12
Q
some cofactors are only transiently associated with a given enzyme molecule, so that they function as ______.
A
Cosubstrates
13
Q
the non-enzyme part of the Co-enzyme is termed
A
Co-factor
14
Q
are inactive form of enzymes. eg: pepsinogen
A
Zymogens or Proenzymes
15
Q
FAD
A
Flavine Adenine Dinucleotide
16
Q
NAD
A
Nicotinamide Adenine Dinucleotide
17
Q
FMN
A
Flavine Mononucleotide
18
Q
involved in carbon dioxide fixation reactions and fatty acid synthesis
A
Biotin
19
Q
coenzyme involved in the transfer of methyl groups;
active in amino acid metabolism
A
Vitamin B12 (cyanocobalamin)
20
Q
needed for cellular and macrocellular syntheses
A
Vitamin E
21
Q
Coenzyme used in electron transport (naphthaquinones and quinones)
A
Vitamin K
22
Q
The 2 Co-factors
A
Co-enzyme
Metal-ion Activator
23
Q
are the inorganic ions of the co-factors
A
Metal-ion Activator
24
Q
contains an apoenzyme and metal ion cofactor
A
Metalloenzyme
25
Vitamin B2
Riboflavin
26
Vitamin B1
Thiamine
27
Vitamin B 12
Cobalamin
28
ascorbic acid
Vitamin C
29
Vitamin B6
Pyridoxine
30
the region of the enzyme that binds the substrate to form enzyme-substrate complex.
Active Site
31
6 major classifications of Enzymes
Hydrolases
Oxidoreductases
Transferases
Lyases
Isomerases
Ligases
32
are also known as synthetase
Ligase
33
are ATP dependent enzymes catalyzing biosynthetic reactions
Synthetases
34
are enzymes catalyzing biosynthesis reaction but do not require ATP
Synthases
35
Class of Enzymes According to CHEMICAL REACTION CATALYZED
Addition of Water Molecules
Transfer of Electrons
Splitting/Forming a C-C Bond
Transfer of a Radical
36
Addition of Water Molecules / Hydrolase:
Carbohydrase
Esterases
Nucleases
Amidases
Proteases
Peptidases
37
aid in the hydrolysis of carbohydrates
Carbohydrase
38
under Carbohydrase: BALMS
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)
39
aid in the hydrolysis of esters
Esterases
40
under Esterases: (LPC)
Lipases (glycerides to fatty acids & glycerol)
Phosphatase (organic phosphates to phosphoric acid)
Choline Esterase/Cholinesterase (acetyl choline to acetic acid & choline)
41
aid in the hydrolysis of nucleic acids
Nucleases
42
under Nucleases:
Polynucleotidases (nucleic acid to nucleotides)
Nucleotidases (nucleotides to nucleosides & phosphoric acid)
Nucleosidase (nucleosides to sugar and purine)
43
aide in the hydrolysis of amides
Amidases
44
under amidases: (UA)
Ureases (urea to ammonia & CO2)
Arginase (arginine to ornithine & urea)
45
aid in the hydrolysis of protein
Proteases
46
under proteases:
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)
47
hydrolyze peptides to simple peptides and amino acids
Peptidases
48
under peptidases: (PCAD)
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)
49
are enzymes which catalyze the removal of hydrogen from a substrate and pass it directly to oxygen
Oxidases
50
Examples of OXIDASES (DCAPT)
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)
51
catalyze the linkage not broken by water; splitting or forming a C-C bond
Desmolases
52
under Desmolases: (DCC)
Decarboxylases
- Carboxylase (alpha keto acids to CO2 & aldehydes)
- Carbonic & Anhydrase (carbonic acid to water & CO2)
53
catalyze the transfer of amino groups from amino acids to ketoacids and promotes the formation of new amino acids.
Transaminases
54
under transaminase: (AG)
Alanine Transaminase
Glutamate Transaminase
55
catalyzes transfer of alpha-amino group from amino acid to pyruvic acid to produce alpha keto acid and alanine
Alanine Transaminase
56
catalyzes transfer of alpha-amino group from amino acid to alpha-ketoglutyaric acid to produce alpha keto & glutamic acid
Glutamate Transaminase
57
all Enzymes are protein EXCEPT
Ribozymes / RNA molecules
58
Enzymes can work /cooperate with non-protein portion called ____?
Co-factors
59
co-factors remain tightly bound to an enzyme
most are metals
metal ion activator (prosthetic group)
60
molecules that enter enzymatic reactions
substances which the enzymes act
Substrates
61
non-protein , required for enzymatic activities
organic / inorganic
Co-factors
62
protein without bound cofactor
aka. APOPROTEIN
APOENZYME
63
active form of enzyme
coenzyme (organic) + apoenzyme
metal ion activator (inorganic) + apoenzyme
Holoenzyme
64
contains apoenzyme and a metal ion co-factor
metalloenzyme
65
organic compounds derived from vitamins
coenzymes
66
FAD (FLAVINE ADENINE DINUCLEOTIDE)
VITAMIN B2 (RIBOFLAVIN)
67
NAD (NICOTINAMIDE ADENINE DINUCLEOTIDE)
NIACINE - VITAMIN B3
COMMONLY FOUND IN VITAMINS
68
PROTEOLYTIC ENZYMES
PEPSIN
ALCALASE
BROMELAINS
PAPAIN
TRYPSIN
SUTILAINS
RENNIN
EREPSIN
STREPTOKINASE
UROKINASE
FIBRINOLYSIN
69
from Sus scrofa, fam suidae
assist in gastric digestion
found in gastric juice
PROTEINS to PROTEASES & PEPTONES
digestive aid of pre-cooked foods
PEPSIN
70
additive to remove protein stains
ALCALASE
71
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
BROMELAINS
72
from latex of Carica Papaya, Caricaceae
relieve symptoms of episiotomy - clean Contact Lenses
meat/Beef tenderizer
SKIN WHITENER
stabilizer for chill proof beer
PAPAIN
73
nonpyrogenic proteolytic enzyme
relieves lower back pain
CHYMOPAPAIN
74
PROTEASES to POLYPEPTIDES & AMINO ACIDS
by pancreas
for wound debridement
TRYPSIN
75
from extract of pancreatic gland of Ox
for ophthalmic solution
CHYMOTRYPSIN
76
from bacillus subtilis
for wound debridement
SUTILAINS
77
coagulated enzyme present in mucous membrane of animal stomach
soluble cassein milk
for cheesemaking
RENNIN
78
intestinal juice
PROTEOSES & PEPTONES to AMINO ACIDS
EREPSIN
79
purified bacterial protein by group C B-hemolytic streptococci
as lyophilized powder
PLASMINOGEN to PLASMIN
STREPTOKINASE
80
human urine or from human kidney cells
PLASMINOGEN to PLASMIN
UROKINASE
81
in blood serum as a protease, profibrinolysin or plasminogen
activate human blood plasma fraction with streptokinase
FIBRINOLYSIN
82
formation of blood clot
THROMBOSIS
83
OXIDIZING ENZYMES (PerTh)
PEROXIDASE
THROMBIN
84
PLANTS!
oxidation reactions cause discoloration of bruised fruits
PEROXIDASE
85
fibrinogen of circulating blood into insoluble fibrin
COAGULATION FACTOR II
THROMBIN
86
CARBOHYDRASE / AMYLOLYTIC ENZYMES
AMYLASE
DIASTASE
AMYLOPSIN
INVERTASE / SUCRASE
ZYMASE
EMULSIN
MYROSIN
AMYLOGLUCOSIDASE
CELLULASE
LACTASE
PECTINASE
HYALURONIDASE
87
in salivary glands
aka. salivary diastase / ptyalin
AMYLASE
88
yellowing white, malt
POTATO to SUGAR
DIASTASE
89
digestive tract of animals
aka. animal diastase
AMYLOPSIN
90
yeast and intestinal juice
SUCROSE to GLUCOSE & FRUCTOSE
CANDIES!!
INVERTASE / SUCRASE
91
MONOSACCHARIDES to ALCOHOL & CO2
ZYMASE
92
ALMONDS!!
EMULSIN
93
white and black mustard
MYROSIN
94
dextrose from starch
AMYLOGLUCOSIDASE
95
COFFEE
CELLULASE
96
lactose crystals ICE CREAM
LACTASE
97
WINES & JUICES
PECTINASE
98
HYALURONIC ACIDS
SPREADING DIFFUSING FACTOR AGENT
HUMAN TESTES/ LOEECHES/SNEK VENOMS
HYALURONIDASE
99
ESTERASES - LUPS
LIPASE
UREASE
PECTASE
STEAPSIN
100
lipolytic enzyme, animal and veggie kingdom
]pancreatic juice of animals
cheese flavor production
LIPASE
101
PECTIN to PECTIDE ACID & METHYL ALCOHOL
PECTASE
102
lipolytic enzyme, digesting dietary fat
STEAPSIN
103
UREA to AMMONIA
SOYBEANS!!!!
UREASE
104
OTHERS???? - CoL-ALip
COLLAGENASE
L-ASPARAGINASE
LIPOXYGENASE
105
clostridium histolyticum
cleaves collagen for ulcers and burns
COLLAGENASE
106
FROM ESCHERICHIA COLI (E. COLI)
for leukemia
L-ASPARAGINASE
107
BREAD - WHITENING
LIPOXYGENASE
108
temporary intermediate compound forms
enzyme - substrate complex
109
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
ACTIVATION ENERGY
110
theories explaining mode of enzyme action
FISCHER'S LOCK AND KEY THEORY
KOSHLAND'S INDUCED FIT THEORY
111
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.
FISCHER'S LOCK AND KEY THEORY
112
in this model, some type of modification is induced in the substrate, enzyme, or both.
modification begins process of reaction.
KOSHLAND'S INDUCED FIT THEORY
113
FACTORS THAT INFLUENCE ENZYME ACTION
Concentration of Substrates
Concentration of Enzymes
Temperature
pH
Presence of Accelerators
Presence of Inhibitors
Environmental Hazards
114
the optimum temperature of enzyme in the body
37 degrees Celsius
115
they activate the enzyme
accelerators
116
have the ability to combine with enzyme in a reversible and irreversible reaction and hence block enzyme catalysis
Inhibitors
117
environmental hazards
Hg (mercury) - phenyl mercuric acetate & methyl mercuric acetate
Cd (cadmium) - cigarette smoke
Pb (lead) - gasoline / yellow-painted pencils
118
in CLINICAL ENZYMOLOGY, Enzymes are commonly used in medicine as:
Analytical tools or reagents for measuring quantities
As index for pathology of diseases
119
in acute pancreatitis, perforated duodenal and peptic ulcers and intestinal obstruction
LIPASE
120
in blood after MI
sensitive indicator in the early stages of myocardial ischemia
Creatine Phosphokinase (CPK)
121
found in skeletal and heart muscle
MM(CK3)
122
found in heart muscles
MM(CK2)
123
found in brain
BB(CK1)
124
in rickets, obstructive jaundice
Alkaline Phosphatase
125
carcinoma of prostate (prostate cancer)
Acid Phosphatase
126
viral heap, heart and skeletal muscle disease
LDH - Lactase Dehydrogenase
127
in Myocardial infarction
AST - Aspartate Transaminase
128
in liver disease
ALT - Alanine Transaminase
129
in liver disease, biliary obstruction (gallstone)
Glutamyl Transferase
130
moderately increase in hepatitis and highly elevated biliary obstruction
5' Nucleotidase
131
use as treatment of pulmonary embolism, coronary artery thrombosis and restoring the patency of intravenous catheters
Urokinase
132
use as treatment of pulmonary embolism, deep vein thrombosis, arterial thrombosis and embolism, arteriovenous cannula acclusion and coronary artery thrombosis
Streptokinase
133
use as treatment of blood clots within the cardiovascular system, exclusive of thrombi of the coronary and cerebral arteries
Fibrinolysin
134
the prosthetic group; makes the enzyme active, "active site"
Conjugated protein
135
used for adjunctive therapy to reduce inflammation and edema
accelerate tissue repair, esp. following episiotomy
Bromelains
136
enzymes used for testing Triglycerides
Lipase
137
enzyme used to test polymerase chain reaction
Reverse Transcriptase
138
The 3 CK isoenzymes:
MM(CK3)
MM(CK2)
BB(CK1)
