Chem ch 19 Flashcards

1
Q

active site is the part of enzyme with…(active in SC)

A

a specific shape and specific chemical make up.

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2
Q

substrate is…

A

a reactant in an enzyme-catalyzed reaction

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3
Q

Specificity of the enzyme is the…(the enzyme must be specific to S or R)

A

limitation of the activity of an enzyme to a specific substrate, specific reaction, or specific type of reaction

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4
Q

specificity

A

limitation of the activity of an enyzme to specific substrate or specific reaction

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5
Q

turnover number

A

10 - 10,000,000 molecules per second. The maximum number of substrates at which an enzyme can act upon per unit of time. ex - catalase is 10 (7)/ per second - very fast

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6
Q

cofactor and co-enzyme

A

non-protein part of an enzyme that is essential for the activity of the enzyme

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7
Q

cofactors are made of what?

A

minerals (metal ions)

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8
Q

co-enzyme is the…(it’s not the co-factor)

A

organic molecule (vitamins)

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9
Q

trace minerals (FFCK MZ)

A

are co-factors - CU2+, Fe2+, Fe3+, K+, Mg2+, Zn2+. They do coordinate covalent bond - covalent that is formed by sharing electrons, but one part is providing 2 electrons. the other is accepting. The act as Lewis acid, accepting electrons.

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10
Q

enzyme nomenclature

A

2 parts: identify the substrate that which the enzyme is acting upon. Describe the reaction. Family ending - ase. ie - pyruvate carboxylase

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11
Q

oxidase

A

adding oxygen

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12
Q

reductase

A

removing O2

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13
Q

dehydrogenase

A

adding or removing H

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14
Q

types of transferase (kin and tran can transfer)

A

A) kinase

B) transaminase

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15
Q

hydrolase (PLLAN your watering)

A

enzymes that catalyze the cleavage of a covalent bond using water

A) lipase
B) protease
C) amylase - sugar
D) nulcease - DNA or RNA
E) ligases
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16
Q

isomerase

A

converting one isomer to another one

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17
Q

lyase (lays is basic math)

A

adding or removing functional group using something other than water

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18
Q

decarboxylase

A

removing COO- and (CO2)

19
Q

deaminase

A

remove amino group

20
Q

dehydrotase

A

removing H2O

21
Q

hydrotase

A

adding H2O

22
Q

ligases (ligase is the ligament to hold SoCal together)

A

linking or bonding 2 substrates together: A) sythetase (using ATP - form product by adding 2 substrates) B) carboxylase

23
Q

models that describe how enzymes work

A

lock and key and induced fit model

24
Q

lock and key

A

when substrate fits into active site of the enzyme as a key fits into a lock

25
Q

induced fit model

A

active site of the enzyme is flexible and it changes it’s shape to fit the substrate

26
Q

abilities of enzymes (ability of enzyme to COPE)

A

1) proximity effect
2) orientation effect
3) catalytic effect
4) energy effect

27
Q

proximity effect

A

enzymes are able to position on the substrate at the active site and bound to the substrate. ex - induced fit model

28
Q

orientation effect

A

enzyme is holding the substrate at the exact distance and exact orientation

29
Q

factors that effect enzyme activity (PETS even effect enzyme activity)

A

1) substrate concentration
2) enzyme concentration
3) temperature effect
4) pH change effect

30
Q

substrate concentration - what is it? (can’t have substrate without rate)

A

concentration of substrate X is rate of biochemical reaction until all of the active sites are fully occupied (enzyme is saturated)

31
Q

enzyme concentration

A

rate of the biochemical reaction is directly proportional to the enzyme concentration

32
Q

temperature effect (at what temp?)

A

most enzymes denature and they lose the activity about 50 - 60 degrees C. high temp is killing the enzyme

33
Q

pH effect

A

moste enzymes have optimum point at normal and/or buffered pH of the environment. most at pH 5 to 9.

34
Q

activation energy (activate the intermediate!)

A

the difference in energy in between the intermediate and the reactant

35
Q

catalysts do what?

A

just lower activation energy point

36
Q

substrate is really just the…

A

reactant

37
Q

R + E —- SE — PE – P + E

A

reaction plus enzyme = product, but the enzyme is still attached to product. it is released later

38
Q

important co-enzymes (B a FAN of co-enzymes)

A

co-enzyme A, B12, FAD, NAD+

39
Q

oxidoreductase

A

catalyze oxidation-reduction reactions of substrate molecules, most commonly addition or removal of oxygen or hydrogen.

40
Q

when looking at substrate and reactant (if it’s on the test) and she asks what reaction, if its the same molecule with different connectivity, it’s…

A

isomerization

41
Q

kinase (think of physio)

A

transferring phosphate group

42
Q

transaminase

A

transferring amino group

43
Q

types of lyase (the lyase-on hides the problems - HDDD)

A

A) decarboxylase
B) deaminase
C) dehydrotase
D) hydrotase