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1
Biologic catalysts that cause reactions in the body to take place. These substance in the body increases the rate of chemical reaction.
ENZYME
2
Characterisitcs of enzymes are capable of ionizing either as acid or as a base
AMPHOTERIC
3
Use to define coenzyme
CO SUBSTRATE
4
Metabolic regulator of enzyme reaction
ACTIVATOR
5
the combined enzyme & coenzyme
HOLOENZYME
6
Acted upon by an enzyme & is converted into a new substance
SUBSTRATE
7
Substance derived from a transformed substrate
PRODUCT
8
Site other than the active site that may lead to either attachment of substrate to the enzymes
ALLOSTERIC SITE
9
Where an inhibitor or an activator can attach to
ACTIVE SITE
10
It inhibits the attachment of substrate to the active site
ALLOSTERIC INHIBITOR
11
These influences the enzyme particularly the sheath of active site.
ALLOSTERIC ACTIVATOR
12
Protein structure refering to the sequence of amino acids joined by peptide bonds to form a polypeptide chain
PRIMARY
13
Protein structure refering to conformation of the segments of polypeptide chain maintained by hydrogen bond. Samples are Alpha-helix; beta-pleated sheet
SECONDARY
14
Protein structure arises from the interactions among side chains/groups of the polypeptide chain. It is Bent and folded structure maintained by _______.
TERTIARY, COVALENT DISULFIDE BOND
15
Protein structure made up of 4 polypeptide units separated bended and folded structures are put together to form a functional unit.
QUARTERNARY
16
Assayed for investigation of cardiac and liver disorders
OXIDOREDUCTASE
17
Gives information about liver damage
TRANSFERASE
18
Splits molecules with water as part of the reaction process
HYDROLASE
19
Hydrolase 3 groups
ESTERASE, PEPTIDASE, GLYCOSIDASE
20
Responsible for splitting molecules or breaking of bonds (C to C; C to O; C to N, etc.) yielding two smaller articles from a large enzyme.
LYASE
21
Assayed in disorders of skeletal muscles
LYASE
22
Responsible for the conversion of one isomer to another
ISOMERASE
23
All reactions are reversible
ISOMERASE
24
Enzymes causing bond formation between two molecules to form larger molecule from two smaller molecules (in the presence of ligases) it became one large molecule
LIGASE
25
In-systematic naming of enzyme, the 1st digit denotes for
CLASS
26
In-systematic naming of enzyme, the 2nd digit denotes for
SUB CLASS
27
In-systematic naming of enzyme, the 3rd digit denotes for
SUBSUB CLASS
28
Multichained enzymes of similar activity. Appear in specific tissue, organ & cell organelle of similar organisms.
ISOENZYME
29
Lactate Dehydrogenase has how many isoenzyme
5
30
Isoenzyme of LDH found in heart, RBC & renal tubules
LDH1, LDH2
31
Isoenzyme of LDH found in liver, skeletal muscles
LDH4, LDH5
32
Enzymes that exert their function in plasma secreted by the liver
PLASMA SPECIFIC
33
Classification of enzyme found only in one location, particularly the cell sap (vacuoles of the cell the storage compartment of the cell which can store protein and sugar
UNILOCULAR ENZYME
34
Classification enzyme found in the Mitochondria & cell sap
BILOCULAR ENZYME
35
commonness between the enzyme and substrate
MOLECULAR COMPATIBILITY
36
the number of enzyme/substrates that can be reacted
SPACE AVAILABILITY
37
enzyme active on a specific substrate
SPECIFICITY
38
TYPES OF ENZYME SPECIFICITY when an enzyme can act and catalyze one unique reaction
ABSOLUTE SPECIFICITY
39
FACTORS THAT AFFECT BINDING OF ENZYME TO SUBSTRATE
ENERGY, MOLECULAR COMPATIBILITY, SPACE AVAILABILITY, SPECIFICITY
40
TYPES OF ENZYME SPECIFICITY when some enzymes act on different substrates belonging to the same group
GROUP SPECIFICITY
41
TYPES OF ENZYME SPECIFICITY an enzyme acts only on the specific isomer
STEREOISOMERIC
42
the enzyme changes in shape during binding to accommodate the substrate
INDUCED FIT MODEL
43
In this reaction, the entire enzyme is bound to substrate and a much higher rate of reaction is obtainedBecause the entire enzyme is present in the form of the complex, there is now no further increasein ES complex conc. No further increment in reaction rate ispossible
ZERO ORDER KINETIC
44
The rate observed reflects the low concentration of the ES complex
FIRST ORDER KINETIC
45
Optimum temperature considered favorable for enzyme activity
37-40
46
the point at w/c the reaction rate is greatest
OPTIMUM PH
47
Pepsin – active at _pH
1.5
48
ALP – active at_pH
10.5
49
ACTIVATORS
IRON, CALCIUM, ZINC, MAGNESIUM
50
Decrease the rate of enzyme reaction
INHIBITOR
51
Is not possible to remove the inhibitor
IRREVERSIBLE INHIBITION
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