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Clinical Chemistry 2 > Chapter 13 - Enzymes > Flashcards

Chapter 13 - Enzymes Flashcards

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1
Q

Enzyme portion

A

Apoenzyme

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2
Q

Digestive enzymes in structurally inactive form

A

Proenzyme/zymogen

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3
Q

Trypsin

A

Hydrolases

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4
Q

Water-free cavity, where the substance on which the enzyme acts interacts with particularly charged amino acid residues

A

Active site

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5
Q

Chymotrypsin

A

Hydrolases

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6
Q

alpha-amylase

A

Hydrolases

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7
Q

Creatinine kinase

A

Transferases

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8
Q

Enzymes contains a specific amino acid sequence

A

Primary structure

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9
Q

Aldolase

A

Lyases

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10
Q

Polypeptide chains twisting

A

Secondary structure

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10
Q

Organic cofactor

A

Coenzyme (NAD)

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11
Q

5-nucleotidase

A

Hydrolases

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12
Q

Cholinesterase

A

Hydrolases

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13
Q

Inorganic cofactors, also called activators

A

Chloride or magnesium ions

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15
Q

May bind regulator molecules and, thereby, be significant to the basic enzyme structure

A

Allosteric site

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16
Q

Elastase-1

A

Hyrolases

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17
Q

Glutathione synthetase

A

Ligase

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18
Q

Folds —> structural cavities

A

Tertiary structure

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19
Q

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bond in ATP or a similar compound

A

Isomerases

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20
Q

Catalyze the interconversion of geometric, optical, or positional isomers

A

Isomerases

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21
Q

Catalyze the transfer of a group other than hydrogen from one substrate to another

A

Transferases

22
Q

More than one polypeptide unit, refers to the spatial relationships between the subunits

A

Quaternary structure

24
Q

Pyruvate kinase

A

Transferases

24
Q

Triacylglycerol lipase

A

Hydrolases

25
Q

Cataylze hydrolysis of various bonds

A

Hydrolases

26
Q

Complete and active system

A

Holoenzyme

27
Q

Catalyze removal of groups from substrates without hydrolysis; the product containing double bonds

A

Lyases

28
Q

Enzyme is subject to posttransitional modification

A

Isoform

30
Q

Enzyme exist in different forms within the same individual

A

Isoenzyme

31
Q

Glycogen phosphorylase

A

Transferases

32
Q

Nonprotein molecule, necessary for enzyme activity

A

Cofactor

32
Q

Coenzyme bound tightly to the enzyme

A

Prosthetic group

33
Q

Catalyze an oxidation-reduction reaction between two substrates

A

Oxidoreductases

34
Q

Enzymes combines with only one substrate

A

Absolute specificity

35
Q

They combine with all substrates containing a particular chemical group (phosphate ester)

A

Group specific

36
Q

Enzymes are specific to chemical bonds

A

Bond specificity

37
Q

Enzymes that predominantly combine with only one optical isomer of a certain compound

A

Stereoisometric specificity

38
Q

A physical binding of a substrate to the active site of an enzyme

A

ES complex

39
Q

The substrate readily binds to free enzyme at a low concentration

A

Substrate concentration

40
Q

The higher the enzyme level, the faster the reaction will proceed because more enzyme is present to bind with substrate

A

Enzyme concentration

41
Q

Changes in pH may denature an enzyme or influence its ionic state, pH range 7.0 - 8.0

A

pH

42
Q

Increase temperature —> Increase the rate of a chemical reaction

Usually at 40C

A

Temperature

43
Q

Metallic Activators

A

Ca2+, Fe2+, Mg2+, Mn2+, Zn2+, K+

44
Q

Nonmetallic activators

A

Br-, Cl-

45
Q

Common coenzymes

A

Nucleotide phosphates and vitamins

46
Q

Increasing coenzyme concentration will increase the velocity of an enzymatic reaction in a manner synonymous with increasing substrate concentration

A

Cofactors

47
Q

Interferes with the reaction

A

Inhibitors

48
Q

Physically bind to the active site for an enzyme, and compete with the substrate for the active site
Inhibitors are reversible

A

Competitive inhibitors

49
Q

Binds an enzyme at a place other than the active, maybe reversible and irreversible

A

Noncompetitive inhibitor

50
Q

Inhibitors binds to this ES-complex

A

Uncompetitive inhibition

51
Q

Acid phosphatase

1) Optimal pH
2) Tissue source
3) Diagnostic significance
4) Most specific substrate
5) Inhibitor
6) Preferred for continuous-monitoring mtds
7) Reference range:
Prostatic ACP
Tartrate-resistant ACP, adults
Children

A

1) 5.0 pH
2) Prostate, bone, liver, spleen, kidney, erythrocytes, and platelets
3) Prostatic carcinoma, Forensic CC(rape cases), Paget’s dse, breast cancer with bine metastases, Gaucher’s dse
4) Thymolphthalein monophosphate (Roy & Hillman)
5) L-tartrate, formaldehyde and cupric ions (RBC)
6) alpha-naphthyl phosphate, 13abson reading and philipps
7) 0-3.5 mg/dL
1. 5-4.5 U/L (37C)
3. 5-9.0 U/L (37C)

52
Q

Alkaline phosphatase

1) Optimal pH
2) Activator
3) Tissue Source
4) Diagnostic significance
5) Continues-monitoring technique
6) Sources of error
7) Most heat labile inhibited by phenylalanine
8) Inhibited by phenylalanine and leucine

A

1) 9.0-10.0 pH
2) Mg2+
3) Liver, bone, intestine, spleen, placenta, kidney
4) Hepatobiliary and bone disorders, Obstructive jaundice, Paget’s dse(osteotic neoformans)
5) Bowers and McComb (p-nitrophenol-yellow) at 405 nm
6) Hemolysis
Increases 3-10% on standing 25C/4C for several hrs
7) Regan
8) Nagao

Clinical Chemistry 2 (1 decks)

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