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Introduction
  • Jef Marc Valencia

  • 問題数 51 • 9/16/2024

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    問題一覧

  • 1

    In-systematic naming of enzyme, the 1st digit denotes for

    CLASS

  • 2

    Acted upon by an enzyme & is converted into a new substance

    SUBSTRATE

  • 3

    Responsible for the conversion of one isomer to another

    ISOMERASE

  • 4

    In-systematic naming of enzyme, the 2nd digit denotes for

    SUB CLASS

  • 5

    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

  • 6

    Biologic catalysts that cause reactions in the body to take place. These substance in the body increases the rate of chemical reaction.

    ENZYME

  • 7

    Assayed in disorders of skeletal muscles

    LYASE

  • 8

    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

  • 9

    In-systematic naming of enzyme, the 3rd digit denotes for

    SUBSUB CLASS

  • 10

    Splits molecules with water as part of the reaction process

    HYDROLASE

  • 11

    FACTORS THAT AFFECT BINDING OF ENZYME TO SUBSTRATE

    ENERGY, MOLECULAR COMPATIBILITY, SPACE AVAILABILITY, SPECIFICITY

  • 12

    Assayed for investigation of cardiac and liver disorders

    OXIDOREDUCTASE

  • 13

    All reactions are reversible

    ISOMERASE

  • 14

    These influences the enzyme particularly the sheath of active site.

    ALLOSTERIC ACTIVATOR

  • 15

    ACTIVATORS

    IRON, CALCIUM, ZINC, MAGNESIUM

  • 16

    Lactate Dehydrogenase has how many isoenzyme

    5

  • 17

    the combined enzyme & coenzyme

    HOLOENZYME

  • 18

    ALP – active at_pH

    10.5

  • 19

    Substance derived from a transformed substrate

    PRODUCT

  • 20

    the point at w/c the reaction rate is greatest

    OPTIMUM PH

  • 21

    commonness between the enzyme and substrate

    MOLECULAR COMPATIBILITY

  • 22

    Is not possible to remove the inhibitor

    IRREVERSIBLE INHIBITION

  • 23

    Site other than the active site that may lead to either attachment of substrate to the enzymes

    ALLOSTERIC SITE

  • 24

    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

  • 25

    Protein structure made up of 4 polypeptide units separated bended and folded structures are put together to form a functional unit.

    QUARTERNARY

  • 26

    The rate observed reflects the low concentration of the ES complex

    FIRST ORDER KINETIC

  • 27

    Gives information about liver damage

    TRANSFERASE

  • 28

    Classification enzyme found in the Mitochondria & cell sap

    BILOCULAR ENZYME

  • 29

    Metabolic regulator of enzyme reaction

    ACTIVATOR

  • 30

    Multichained enzymes of similar activity. Appear in specific tissue, organ & cell organelle of similar organisms.

    ISOENZYME

  • 31

    Hydrolase 3 groups

    ESTERASE, PEPTIDASE, GLYCOSIDASE

  • 32

    Isoenzyme of LDH found in heart, RBC & renal tubules

    LDH1, LDH2

  • 33

    the enzyme changes in shape during binding to accommodate the substrate

    INDUCED FIT MODEL

  • 34

    the number of enzyme/substrates that can be reacted

    SPACE AVAILABILITY

  • 35

    enzyme active on a specific substrate

    SPECIFICITY

  • 36

    Characterisitcs of enzymes are capable of ionizing either as acid or as a base

    AMPHOTERIC

  • 37

    Use to define coenzyme

    CO SUBSTRATE

  • 38

    Decrease the rate of enzyme reaction

    INHIBITOR

  • 39

    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

  • 40

    Pepsin – active at _pH

    1.5

  • 41

    Where an inhibitor or an activator can attach to

    ACTIVE SITE

  • 42

    Protein structure refering to conformation of the segments of polypeptide chain maintained by hydrogen bond. Samples are Alpha-helix; beta-pleated sheet

    SECONDARY

  • 43

    Protein structure refering to the sequence of amino acids joined by peptide bonds to form a polypeptide chain

    PRIMARY

  • 44

    Optimum temperature considered favorable for enzyme activity

    37-40

  • 45

    Isoenzyme of LDH found in liver, skeletal muscles

    LDH4, LDH5

  • 46

    TYPES OF ENZYME SPECIFICITY when an enzyme can act and catalyze one unique reaction

    ABSOLUTE SPECIFICITY

  • 47

    Enzymes that exert their function in plasma secreted by the liver

    PLASMA SPECIFIC

  • 48

    TYPES OF ENZYME SPECIFICITY an enzyme acts only on the specific isomer

    STEREOISOMERIC

  • 49

    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

  • 50

    It inhibits the attachment of substrate to the active site

    ALLOSTERIC INHIBITOR

  • 51

    TYPES OF ENZYME SPECIFICITY when some enzymes act on different substrates belonging to the same group

    GROUP SPECIFICITY