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

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
what does biotin carry
CO2, carboxylation
26
what does tratrhtydrofolate amino acid metabolism carry
1 carbon unit, to carbon or sulfur
27
what does S-adenosylmethionin carry
methyl to oxygen or nitrogen
28
what does pyridoxal phosphate react with to make
amines, NH2, NH, to make amino acids
29
what does thiamin pyrophosphate react with to make
aldehydes and ketones to make decarboxylation at the R group
30
what are the 4 protease classifications
cysteine, aspartic, metalloproteases, serine
31
cysteine proteases
acitve site cysteine. Ex. papain (meat tenderizer), cathespin B (lysosomes0
32
aspartic proteases
Active site aspartate examples: Pepsin, HIV protease Active at low pH
33
metalloproteases
active site metal ion required, usually Zn sometimes Co | Examples: Collagenase, Matrix metalloprtoeases
34
serine proteases
conserved active site catalytic triad: Asp, Ser, His ex. Trypsin chtmotrypsin, elastase, thrombin, Inhibited by serpins: Alpha-1-antitrypsin
35
what are serpins
serine protease inhibitors
36
what do serpins do
they are irreversible "suicide inhibitors" Serpin protein cleavage site recognized by specific proteases, at the covalent intermediat step, the serpin irreversibly changes conformation
37
what are two clinically important examples of serpin
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