this Flashcards

1
Q

transposons

A

segments of DNA, 700 to 40,000 bp in length,
that transpose (move) themselves from one location in a DNA
molecule to another location in the same or a different molecule.

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2
Q

transposition

A

The result of the action of a transposon is termed

transposition; in effect it is a kind of frameshift insertion . rare

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3
Q

compelx transpososns

A

contain one or more genes not connected

with transposition, such as genes for antibiotic resistance

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4
Q

IS

A

The simplest transposons, called insertion sequences (IS),
consist of no more than two inverted repeats and a gene that
encodes the enzyme transposase (Figure 7.38a). Transposase recognizes
its own inverted repeat in a target site, cuts the DNA at that site, and inserts the transposon (or a copy of it) into the
DNA molecule at that site

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5
Q

hydrolase

A

catabolize molecules by adding water in a decomposition
process known as hydrolysis. Hydrolases are
used primarily in the depolymerization of macromolecules.

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6
Q

isomerase

A

rearrange the atoms within a molecule but do
not add or remove anything (so they are neither catabolic
nor anabolic).

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7
Q

ligase / polymearses

A

join two molecules together (and are

thus anabolic). They often use energy supplied by ATP

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8
Q

lyase

A

split large molecules (and are thus catabolic) without

using water in the process.

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9
Q

oxidoreductases

A

remove electrons from (oxidize) or add
electrons to (reduce) various substrates. They are used in
both catabolic and anabolic pathways

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10
Q

transferase

A

transfer functional groups btwn molecules. can be anabolic

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11
Q

apoenzymes

A

Many protein enzymes are complete in themselves, but others
are composed of both protein and nonprotein portions.
The proteins in these combinations are called apoenzymes

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12
Q

cofactors

A

Apoenzymes are inactive if they are not bound
to one or more of the nonprotein substances called cofactors.
Cofactors are either inorganic ions (such as iron, magnesium,
zinc, or copper ions) or certain organic molecules called coenzymes
1ko@en´zıms). All coenzymes are either vitamins or contain
vitamins, which are organic molecules that are required for
metabolism but cannot be synthesized by certain organisms (especially
mammals).

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13
Q

hologneyzme

A

The binding of an apoenzyme and its cofactor(s) forms an active
enzyme, called a holoenzyme

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14
Q

ribozymes

A

Not all enzymes are proteinaceous; some are RNA molecules
called ribozymes. In eukaryotes, ribozymes process other
RNA molecules by removing sections of RNA and splicing the remaining
pieces together.

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15
Q

allosteric

A

(a) Allosteric
(noncompetitive) inhibition results from a change in the shape of the
active site when an inhibitor binds to an allosteric site. (b) Allosteric
activation results when the binding of an activator molecule to an
allosteric site causes a change in the active site that makes it capable
of binding substrate.

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16
Q

competitive inhibitors

A

Competitive inhibitors are shaped such that they fit into an
enzyme’s active site and thus prevent the normal substrate from
binding

17
Q

reversible competition can be overcome by

A

an increase in the
concentration of substrate molecules, increasing the likelihood
that active sites will be filled with substrate instead of inhibitor

18
Q

feedbak inhibition

A

The end-product of a metabolic
pathway allosterically inhibits the initial step, shutting down the
pathway

19
Q

fermentation

A

Utilizes glycolysis then converts pyruvic acid into another compound (organic waste products)

20
Q

glycolysis

A

Occurs in cytoplasm of most cells

Involves splitting of a six-carbon glucose into two three-carbon sugar molecules

Direct transfer of phosphate between two substrates occurs four times – substrate level phosphorylation

Net gain of two ATP molecules, two molecules of NADH, and precursor metabolite pyruvic acid

21
Q

glycolysis stages

A

involving 10 total steps

Energy-Investment Stage

Lysis Stage

Energy-Conserving Stage

22
Q

cellular repsiration

A

Resultant pyruvic acid completely oxidized to produce ATP by a series of redox reactions

23
Q

cell resp stages

A

Synthesis of acetyl-CoA

Krebs cycle

Final series of redox reactions
(electron transport chain)

24
Q

krebs cycle

A

Great amount of energy remains in bonds of acetyl-CoA

The Krebs cycle transfers much of this energy to coenzymes NAD+ and FAD

Occurs in cytoplasm of prokaryotes and in matrix of mitochondria in eukaryotes

25
Q

ETC where

A

Located in cristae of eukaryotes and in the cytoplasmic membrane of prokaryotes

26
Q

ETC

A

The most significant production of ATP occurs through stepwise release of energy from series of redox reactions known as an electron transport chain

consists of series of membrane-bound carrier molecules that pass electrons from one to another and ultimately to final electron acceptor

Energy from electrons used to pump protons (H+) across the membrane, establishing a proton gradient

27
Q

ubiquinones

A

lipid-soluble, nonprotein
carriers that are so named because they are ubiquitous in
cells. Ubiquinones are derived from vitamin K. In mitochondria,
the ubiquinone is called coenzyme Q.

28
Q

metal cotaining proteins

A

a mixed group of integral
proteins with a wide-ranging number of iron, sulfur, and
copper atoms that can alternate between the reduced and
oxidized states

29
Q

flavorproteins

A

Flavoproteins are integral membrane proteins, many of

which contain flavin, a coenzyme derived from riboflavin (vit b2)

30
Q

cycothcromes

A

integral proteins associated
with heme, which is the same iron-containing, nonprotein,
pigmented molecule found in the hemoglobin of blood.

31
Q

chemiosmosis

A

Chemiosmosis is a general term for the use of ion gradients
to generate ATP; that is, ATP is synthesized utilizing energy
released by the flow of ions down their electrochemical gradient
across a membrane.

32
Q

oxidativephos

A

Protons, propelled by proton motive force, flow down electrochemical gradient through ATP synthases (protein channels) that phosphorylate ADP to ATP

Called oxidative phosphorylation because proton gradient created by oxidation of components of ETC