Chapter 10-Introduction to Metabolism Flashcards

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1
Q

biodegradation

A

catabolism

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2
Q

biosynthesis

A

anabolism

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3
Q

breakdown of a larger molecule into smaller ones, breaks covalent bonds and releases energy, exergonic, enzyme catalyzed, most are oxidations and precursors for anabolism

A

catabolism

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4
Q

the synthesis of a larger molecule from a smaller one, creates many new covalent bonds, requires energy input, endergonic, enzyme catalyzed, mostly seen in reductions

A

anabolism (biosynthesis)

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5
Q

What 3 types of work must microbial cells do?

A

(1) chemical work- synthesis of complex molecules
(2) transport work- up take of nutrients, elimination of wastes and ion balance
(3) mechanical work- cell motility and movement of structures within cells

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6
Q

changes in matter of a system

A

thermodynamics

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7
Q

energy can neither be created or destroyed, total energy in the universe remains constant

A

first law of thermodynamics

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8
Q

physical and chemical processes show disorder

A

second law of thermodynamics

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9
Q

amount of disorder or randomness in a system

A

entropy

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10
Q

amount of heat needed to raise one gram of water from 14.5 to 15.5 C

A

calorie

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11
Q

units of work capable of being done by a unit of energy

A

joule

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12
Q

when delta G is negative, ___________

A

the reaction is spontaneous

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13
Q

when delta G is positive, ___________

A

the reaction is not spontaneous

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14
Q

rate of forward reaction is equal to rate of reverse reaction

A

equilibrium

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15
Q

expresses the equilibrium concentrations of products and reactants to one another

A

equilibrium constant (Keq)

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16
Q

high energy molecule, exergonic breakdown to ATP coupled with endergonic reactions to increase favorability

A

role of ATP in metabolism

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17
Q

transfer of electrons, from donor to acceptor, transfer of energy with electrons

A

redox reactions

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18
Q

loss of electrons or an H atom, becomes more positive, exergonic

A

oxidation

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19
Q

gain of electrons or an H atom, becomes less positive, endergonic

A

reduction

20
Q

tendency of a compound to donate or gain electrons, standard condition expressed as volts, more negative = better donor, more positive = better acceptor

A

standard redox potential

21
Q

electron carrier, 1st electron carrier has the most energy, potential energy is stored in first redox couple is released and used as ATP, 1st carrier is reduced and electrons move to next carrier

A

electron transport chain

22
Q

NAD, NADP, NADH

A

electron carriers

23
Q

use iron to transfer electrons (part of heme group)

A

cytochromes

24
Q

organic molecules, serve as catalysts, increase the rate of reaction, protein catalysts are specific to the reaction

A

enzymes

25
Q

increases the rate of reaction without permanent alteration

A

catalyst

26
Q

reacting molecule

A

substrate

27
Q

formed by reaction

A

product

28
Q

protein component of an enzyme

A

apoenzyme

29
Q

loosely attached

A

coenzyme

30
Q

firmly attached

A

prosthetic group

31
Q

holoenzyme

A

loosely attached

32
Q

energy required to form a transition state complex

A

activation energy

33
Q

increasing concentrations of substrates at the active site of an enzyme, proper orientation of substrates to quickly from transition state complex

A

how to lower Ea

34
Q

What environmental conditions effect enzyme activity?

A

substrate concentration, pH, temperature

35
Q

directly competes with binding of substrate to the active site

A

competitive inhibition

36
Q

binds enzyme at site other than active site

A

non-competitive inhibition

37
Q

discovered by Cech and Altman, RNA molecules that can catalyze a reaction, self splicing, self replication, and catalyze peptide bond formation

A

ribozymes

38
Q

differential in localization of enzymes and metabolites

A

metabolic channeling

39
Q

includes metabolic channeling, can generate marked variations in metabolic concentration

A

compartmentation

40
Q

allosteric regulation and covalent modification

A

post translational regulation

41
Q

most regulatory enzymes, small molecule that alters activity (bonds noncovalently at regulatory site, changes shape of enzyme and alters activity of catabolic site), positive effector increases enzyme activity, negative effector inhibits the enzyme

A

allosteric regulation

42
Q

reversible on/off switch, add/remove chemical group, respond to more stimuli in varied and sophisticated ways, regulation of enzyme that catalyze covalent modifications, add a second level of control

A

covalent modifications of enzymes

43
Q

aka end product inhibition, inhibition of 1 or more critical enzymes in a pathway, each end product regulates own branch of pathway, each end product regulates initial pacemaker enzyme

A

feedback inhibition

44
Q

catalyzes slowest rate limiting reaction of pathway

A

pacemaker enzyme

45
Q

different enzymes that catalyze same reaction

A

isoenzymes