B2-075 - Enzyme Nomencalture Flashcards

1
Q

Lysozyme

A

Enzymes that catalyze the same chemical reaction but reaction rates differ often as well as tissues

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2
Q

Class 1

A

oxidoreductases

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3
Q

What are common oxidoreductase coenzymes

A

NADPH, NADH, FADH2

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4
Q

Common oxidoreductase enzyme names

A

Dehydrogenase, peroxidase, Reductase

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5
Q

Special names of oxidoreductase

A

oxidase, hydroxylase, cytochrome p450

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6
Q

What is cytochrome P450

A

an oxidoreductases

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7
Q

Class 2

A

Transferases

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8
Q

What is the enzyme name typically of transferases

A

Which chemical group is transferred or what chemical group is synthesized

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9
Q

what do glycosyl, methyl, carbonyl, and acyl referring to

A

Glycosyl - carbohydrate
methyl - CH3
carbonyl - carbon
acyl - fatty acids

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10
Q

what are some special names of transferases

A

aminotransferases, kinase (transfers a phosphate group usually from ATP), synthase (Indicates what kind of product is formed like glycogen synthase)

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11
Q

class 3

A

Hydrolase

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12
Q

What do hydrolases do

A

split bonds by splitting water, many common names do not mention hydro

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13
Q

common names of hydrolases that don’t mention hydro

A

protease, esterase, phosphates, peptides, urease

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14
Q

class 4

A

lyase

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15
Q

what are lyases

A
catch all class
cleave C-C, C-O, C-S, C-N bonds by means other than oxidation or hydrolysis 
Form C=C bonds by removing H2O from COH-CH
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16
Q

examples of common names of isomerases

A

epimerase, racemase, mutase

17
Q

Class 6

A

ligase

18
Q

what do ligaes do

A

form C-C, C-S, C-O and C-N bonds, require ATP or other nucelotides

19
Q

what is another common name of ligases

A

synthetase

20
Q

What groups does ATP/ADP/AMP carry

A

phosphorylation groups, chemical energy, protein phosphorylation

21
Q

What groups does NADH/NAD+ carry

A

shuttle electrons for redox of biological fuels, help produce ATP

22
Q

what group sdo NADPH/NADP+ carry

A

shuttle electrons for oxidation in biosynthesis reactions

23
Q

What groups do FADH2,FAD/FMNH2/FMN carry

A

shuttle electrons for redox of biological fuels, more powerful than NADs, always bound to a protein

24
Q

what does coenzyme A carry

A

Acyl groups

25
Q

what does biotin carry

A

CO2, carboxylation

26
Q

what does tratrhtydrofolate amino acid metabolism carry

A

1 carbon unit, to carbon or sulfur

27
Q

what does S-adenosylmethionin carry

A

methyl to oxygen or nitrogen

28
Q

what does pyridoxal phosphate react with to make

A

amines, NH2, NH, to make amino acids

29
Q

what does thiamin pyrophosphate react with to make

A

aldehydes and ketones to make decarboxylation at the R group

30
Q

what are the 4 protease classifications

A

cysteine, aspartic, metalloproteases, serine

31
Q

cysteine proteases

A

acitve site cysteine. Ex. papain (meat tenderizer), cathespin B (lysosomes0

32
Q

aspartic proteases

A

Active site aspartate
examples: Pepsin, HIV protease
Active at low pH

33
Q

metalloproteases

A

active site metal ion required, usually Zn sometimes Co

Examples: Collagenase, Matrix metalloprtoeases

34
Q

serine proteases

A

conserved active site catalytic triad: Asp, Ser, His
ex. Trypsin chtmotrypsin, elastase, thrombin,
Inhibited by serpins: Alpha-1-antitrypsin

35
Q

what are serpins

A

serine protease inhibitors

36
Q

what do serpins do

A

they are irreversible “suicide inhibitors”
Serpin protein cleavage site recognized by specific proteases, at the covalent intermediat step, the serpin irreversibly changes conformation

37
Q

what are two clinically important examples of serpin

A

Anti thrombin
- regulated by heparin like molecules
Alpha1 anti trypsin
- inhibits neutrophil elastase in lungs, inactivated by cigarette smoke
- low levels predispose towards empyhsema and cirrhosis