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CHEM 46 > CHEM 46 FINALS > Flashcards

CHEM 46 FINALS Flashcards

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1
Q

a family of substances that are insoluble in water but
soluble in nonpolar solvents and solvents of low polarity,
such as diethyl ether.

A

Lipids

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2
Q
  • Fatty acid with a carbon chain in which all C-C bonds are single bonds
  • Numbering starts from the end of -COOH group
  • Structural notation: it indicates number of C atoms
  • Example - Lauric acid has 12 C atoms and no double bonds = (12:0)
A

Saturated Fatty Acid

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2
Q

A polyunsaturated fatty acid is a fatty acid with a carbon chain in which
two or more carbon–carbon double bonds are present.

A

Polyunsaturated fatty acid

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3
Q

A monounsaturated
fatty acid is a fatty acid with a
carbon chain in which one carbon–
carbon double bond is present.

A

Unsaturated Fatty Acid

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4
Q

an unsaturated fatty acid with its
endmost double bond six carbon atoms away from its
methyl end.

A

Omega (ω)-6 fatty acid

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4
Q

An unsaturated fatty acid with its
endmost double bond three carbon atoms away from
its methyl end.

A

Omega (ω)-3 fatty acids

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5
Q

The number of bends in a fatty acid chain increase as the number of double bonds increase.

A

Space-filling molecules

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6
Q

are triesters of glycerol and long-chain carboxylic acids called fatty acids

A

Triglycerides

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7
Q

triglycerides also called

A

triacylglycerols

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8
Q

Two Types of Triacylglycerols

A

Simple Triacylglycerols
Mixed Triacylglycerols

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9
Q

Three identical fatty acids ar esterified
– Naturally occurring simple triacylglycerols are rare

A

Simple Triacylglycerols

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10
Q

A triester formed from theesterification of
glycerol with more than one kind of fatty acid
– In nature mostly mixed triacylglycerols are found and are
different even from the same source depending on the feed, e.g., corn,
peanut and wheat -fed cows have different triacylglycerols

A

Mixed Triacylglycerols

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11
Q

Amixture of triglycerides containing a high proportion of long-chain, saturated fatty acid

A

Fat

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11
Q

A mixture of triglycerides containing a high proportion of long-chain unsaturated fatty acid or short-chain, saturated fatty acid

A

Oil

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12
Q

base-promoted hydrolysis of fats and oils producing glycerol and
a mixture of fatty acid salts
called soaps

A

Saponification

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12
Q

a lipid
that contains two fatty acids and a
phosphate group esterified to a
glycerol molecule and an alcohol
esterified to the phosphate group.

A

glycerophospholipid

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13
Q

the third major class of lipids which are compounds containing the following
ring system

A

Steroids

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14
Q

Carriers of Cholesterol

A

Lipoproteins

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14
Q

The most abundant steroid in the human body, and the most important, is
cholesterol

A

Cholesterol

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15
Q

oxidation products of cholesterol

A

Bile salts

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16
Q

organic compound that acts as a catalyst for
biochemical reactions

A

Enzymes

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17
Q

composed only of protein (amino acid chains)

A

Simple enzymes

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18
Q

has a nonprotein part (cofactor) in addition to the
protein part (apoenzyme)

A

Conjugated Enzymes

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18
Q

the reactant in an enzyme-catalyzed reaction or the
substance upon which the enzyme acts

A

Substrate

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18
Q

can be a small organic
molecule (coenzyme)
or an inorganic ion
(Zn2+, Fe2+
, etc.)

A

Cofactors

19
Q

– named based on the type of reaction catalyzed and
substrate identity

A

Nomenclature and Classification of Enzymes

19
Q

catalyze redox reactions

A

Oxidoreductases

19
Q

catalyze the transfer of a functional group from
one molecule to another

A

Transferases

19
Q

catalyze the addition of two groups to a double
bond or the removal of 2 groups from adjacent
atoms to create a double bond

A

Lyases

20
Q

catalyze hydrolysis reaction in which the addition
of water molecule to a bond causes the bond to
break

A

Hydrolases

20
Q

catalyze isomerization (rearrangement of atoms)
reactions

A

Isomerases

20
Q

catalyze the joining of two molecules with the help
of ATP

A

Ligases or Synthetases

21
Q

a relatively small part of an enzyme’s structure involved in
catalysis

A

Enzyme Active Site

21
Q

intermediate formed when a substrate
binds to the active site

A

Enzyme-Substrate Complex

22
Q

– active site has a fixed, rigid geometrical
conformation

A

Lock-and-Key Model

22
Q

enzyme will catalyze a particular
reaction for only one substrate

A

Absolute Specificity

22
Q

active site changes shape to accommodate a substrate

A

Induced-Fit Model

23
Q

enzyme can distinguish between
stereoisomers

A

Stereochemical Specificity

24
Q

involves structurally similar
compounds that have the same
functional groups

A

Group Specificity

25
Q

– involves a particular type of bond
– the most general

A

Linkage Specificity

26
Q

Four Factors Affecting Enzyme Activity

A
  1. Temperature
  2. pH
  3. Substrate Concentration
  4. Enzyme Concentration
26
Q

a measure of the rate at which an enzyme converts
substrate to products
in a biochemical reaction

A

Enzyme Activity

27
Q

– rate increases as temperature increases,
however
– when temperature increases beyond
“optimum temperature”, enzyme
starts to denature and rate drastically
decreases

A

Temperature

28
Q

most enzymes exhibit maximum activity
over a very narrow pH range (7.0 – 7.5)
– “optimum pH” is where the enzyme
exhibits maximum activity

A

ph

28
Q

– Enzyme activity increases up to a certain substrate
concentration and thereafter remains constant
– the activity pattern is called a
“saturation curve”

A

Substrate Concentration

29
Q

– number of substrate molecules transformed
per minute by one molecule of enzyme under
optimum conditions of temperature, pH, and saturation.

A

Turnover Number

29
Q

– the concentration of substrate in a reaction is
much higher than that of the enzyme
– greater the enzyme
concentration, the greater the reaction rate

A

. Enzyme Concentration

30
Q

The rates of enzyme-catalyzed reactions can be
decreased by a group of substances called inhibitors.

A

Enzyme Inhibition

31
Q

– a substance that slows or stops the normal catalytic
function of an enzyme by binding to it
– has three (3) modes: reversible competitive inhibition,
reversible non-competitive inhibition, and irreversible
inhibition

A

Enzyme Inhibitor

32
Q

a molecule that sufficiently resembles an enzyme
substrate in shape and charge distribution
competes with the substrate for occupancy of the
enzyme’s active site

A

Reversible Competitive Inhibition

33
Q

a molecule decreases enzyme activity by binding to a
site on an enzyme other than the active site

A

Reversible Noncompetitive Inhibition

33
Q

– responsible for regulating many cellular processes
– an enzyme with two or more protein chains (quaternary
structure) and two kinds of binding sites (substrate and
regulator)

A

Allosteric Enzymes

33
Q

– a molecule inactivates enzyme by forming a strong
covalent bond to an amino acid side-chain group at
the enzyme’s active site
– enzyme is permanently deactivated

A

Irreversible Inhibition

34
Q

a process in which activation or inhibition of the first
reaction in a reaction sequence is controlled by a product of the reaction sequence

A

Feedback Control

34
Q

based on the production of enzymes in an inactive
form (zymogens)

A

Proteolytic Enzymes and Zymogens

35
Q

catalyze the breaking of
peptide bonds that maintain the primary structure
of a protein

A

proteolytic enzymes

36
Q

enzyme activity is altered by covalently modifying the
structure of the enzyme through attachment of a
chemical group to or removal of a chemical group from
a particular amino acid within the enzyme’s structure

A

Covalent Modification of Enzymes

36
Q
A
36
Q
A
36
Q
A
37
Q
A

CHEM 46 (1 decks)

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