CHEM 46 FINALS Flashcards

(61 cards)

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
can be a small organic molecule (coenzyme) or an inorganic ion (Zn2+, Fe2+ , etc.)
Cofactors
19
– named based on the type of reaction catalyzed and substrate identity
Nomenclature and Classification of Enzymes
19
catalyze redox reactions
Oxidoreductases
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catalyze the transfer of a functional group from one molecule to another
Transferases
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catalyze the addition of two groups to a double bond or the removal of 2 groups from adjacent atoms to create a double bond
Lyases
20
catalyze hydrolysis reaction in which the addition of water molecule to a bond causes the bond to break
Hydrolases
20
catalyze isomerization (rearrangement of atoms) reactions
Isomerases
20
catalyze the joining of two molecules with the help of ATP
Ligases or Synthetases
21
a relatively small part of an enzyme’s structure involved in catalysis
Enzyme Active Site
21
intermediate formed when a substrate binds to the active site
Enzyme-Substrate Complex
22
– active site has a fixed, rigid geometrical conformation
Lock-and-Key Model
22
enzyme will catalyze a particular reaction for only one substrate
Absolute Specificity
22
active site changes shape to accommodate a substrate
Induced-Fit Model
23
enzyme can distinguish between stereoisomers
Stereochemical Specificity
24
involves structurally similar compounds that have the same functional groups
Group Specificity
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– involves a particular type of bond – the most general
Linkage Specificity
26
Four Factors Affecting Enzyme Activity
1. Temperature 2. pH 3. Substrate Concentration 4. Enzyme Concentration
26
a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction
Enzyme Activity
27
– rate increases as temperature increases, however – when temperature increases beyond “optimum temperature”, enzyme starts to denature and rate drastically decreases
Temperature
28
most enzymes exhibit maximum activity over a very narrow pH range (7.0 – 7.5) – “optimum pH” is where the enzyme exhibits maximum activity
ph
28
– Enzyme activity increases up to a certain substrate concentration and thereafter remains constant – the activity pattern is called a “saturation curve”
Substrate Concentration
29
– number of substrate molecules transformed per minute by one molecule of enzyme under optimum conditions of temperature, pH, and saturation.
Turnover Number
29
– the concentration of substrate in a reaction is much higher than that of the enzyme – greater the enzyme concentration, the greater the reaction rate
. Enzyme Concentration
30
The rates of enzyme-catalyzed reactions can be decreased by a group of substances called inhibitors.
Enzyme Inhibition
31
– 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
Enzyme Inhibitor
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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
Reversible Competitive Inhibition
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a molecule decreases enzyme activity by binding to a site on an enzyme other than the active site
Reversible Noncompetitive Inhibition
33
– 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)
Allosteric Enzymes
33
– 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
Irreversible Inhibition
34
a process in which activation or inhibition of the first reaction in a reaction sequence is controlled by a product of the reaction sequence
Feedback Control
34
based on the production of enzymes in an inactive form (zymogens)
Proteolytic Enzymes and Zymogens
35
catalyze the breaking of peptide bonds that maintain the primary structure of a protein
proteolytic enzymes
36
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
Covalent Modification of Enzymes
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