BIOLOGICAL CHEMISTRY
Biochemistry. Biochemistry is the study of the
chemical substances found in living systems and the
chemical interactions of these substances with each
other (Section 18.1).
Carbohydrates. Carbohydrates are polyhydroxy
aldehydes, polyhydroxy ketones, or compounds that
yield such substances upon hydrolysis. Plants contain
large quantities of carbohydrates produced via
photosynthesis (Section 18.2).
Carbohydrate classification. Carbohydrates are
classified into four groups: monosaccharides,
disaccharides, oligosaccharides, and polysaccharides
(Section 18.3).
Chirality and achirality. A chiral object is not
identical to its mirror image. An achiral object is
identical to its mirror image (Section 18.4).
Chiral center. A chiral center is an atom in a
molecule that has four different groups tetrahedrally
bonded to it. Molecules that contain a single chiral
center exist in a left-handed and a right-handed form
(Section 18.4).
Stereoisomerism. The atoms of stereoisomers are
connected in the same way but are arranged
differently in space. The major causes of
stereoisomerism in molecules are structural rigidity
and the presence of a chiral center (Section 18.5).
Enantiomers and diastereomers. Two types of
stereoisomers exist: enantiomers and diastereomers.
Enantiomers have structures that are
nonsuperimposable mirror images of each other.
Enantiomers have identical achiral properties but
different chiral properties. Diastereomers have
structures that are not mirror images of each other
(Section 18.5).
Fischer projection formulas. Fischer projection
formulas are two-dimensional structural formulas
used to depict the three dimensional shapes of
molecules with chiral centers (Section 18.6).
Chirality of monosaccharides. Monosaccharides are
classified as D or L stereoisomers on the basis of the
configuration of the chiral center farthest from the
carbonyl group (Section 18.6).
Optical activity. Chiral compounds are optically
active—that is, they rotate the plane of polarized
light. Enantiomers rotate the plane of polarized light
in opposite directions. The prefix (+) indicates that
the compound rotates the plane of polarized light in a
clockwise direction, whereas compounds that rotate
the plane of polarized light in a counterclockwise
direction have the prefix (-) (Section 18.7).
Classification of monosaccharides.
Monosaccharides are classified as aldoses or ketoses
on the basis of the type of carbonyl group present.
They are further classified as trioses, tetroses,
pentoses, etc. on the basis of the number of carbon
atoms present (Section 18.8).
Important monosaccharides. Important
monosaccharides include glucose, galactose, fructose,
and ribose. Glucose and galactose are aldohexoses,
fructose is a ketohexose, and ribose is an aldopentose
(Section 18.9).
Cyclic monosaccharides. Cyclic monosaccharides
form through an intramolecular reaction between the
carbonyl group and an alcohol group of an open-
chain monosaccharide. These cyclic forms
predominate in solution (Section 18.10).
Haworth projection formulas. Haworth projection
formulas are two-dimensional structural
representations used to depict the three-dimensional
structure of a cyclic form of a monosaccharide
(Section 18.11).
Reactions of monosaccharides. Five important
reactions of monosaccharides are (1) oxidation to an
acidic sugar (2) reduction to a sugar alcohol (3)
glycoside formation (4) phosphate ester formation
and (5) amino sugar formation (Section 18.12).
Disaccharides. Disaccharides are glycosides formed
from the linkage of two monosaccharides. The most
important disaccharides are maltose, cellobiose,
lactose, and sucrose. Each of these has at least one
glucose unit in its structure (Section 18.13).
Oligosaccharides. Oligosaccharides are
carbohydrates that contain three to ten
monosaccharide units covalently bonded to each
other. Two important naturally occurring
oligosaccharides are raff nose and stachyose (Section
18.14).
Polysaccharides. Polysaccharides are polymers in
which monosaccharides are the monomers. In
homopolysaccharides, only one type of monomer is
present. Two or more monosaccharide monomers are
present in heteropolysaccharides. Storage
 BIOLOGICAL CHEMISTRY
polysaccharides (starch, glycogen) are storage
molecules for monosaccharides. Structural
polysaccharides (cellulose, chitin) serve as structural
elements in plant cell walls and animal exoskeletons
(Sections 18.15 to 18.18).
Glycolipids and glycoproteins. Glycolipids and
glycoproteins are molecules in which
oligosaccharides are attached through glycosidic
linkages to lipids and proteins, respectively. Such
molecules often govern how cells of differing
function interact with each other (Section 18.20).
Lipids. Lipids are a structurally heterogeneous group
of compounds of biochemical origin that are soluble
in nonpolar organic solvents and insoluble in water.
Lipids are divided into five major types on the basis
of biochemical function: energy storage lipids,
membrane lipids, emulsification lipids, messenger
lipids, and protective coating lipids (Section 19.1).
Types of fatty acids. Fatty acids are monocarboxylic
acids that contain long, unbranched carbon chains.
The carbon chain may be saturated,
monounsaturated, or polyunsaturated. Length of
carbon chain, degree of unsaturation, and location of
the unsaturation influence the properties of fatty
acids. Omega-3 and omega-6 fatty acids are
unsaturated fatty acids with the endmost double bond
three and six carbons, respectively, away from the
methyl end of the carbon chain (Section 19.2).
Triacylglycerols. Triacylglycerols are energy-
storage lipids formed by esterification of three fatty
acids to a glycerol molecule. Fats are triacylglycerol
mixtures that are solids or semi-solids at room
temperature; they contain a relatively high percentage
of saturated fatty acid residues. Oils are
triacylglycerol mixtures that are liquids at room
temperature; they contain a relatively high percentage
of unsaturated fatty acid residues (Section 19.4).
Phospholipids. Phospholipids are membrane lipids
that contain one or more fatty acids, a phosphate
group, and a platform molecule to which the fatty
acid(s) and phosphate group are attached, and an
alcohol attached to the phosphate group. The
platform molecule is either glycerol
(glycerophospholipids) or sphingosine
(sphingophospholipids). Phospholipids have a “head
and two tails” structure. Lecithins, cephalins, and
sphingomyelins are types of phospholipids (Section
19.7).
Sphingoglycolipids. Sphingoglycolipids are
membrane lipids in which a fatty acid and a mono- or
oligosaccharide are attached to the platform molecule
sphingosine. Cerebrosides and gangliosides are types
of sphingoglycolipids (Section 19.8).
Cholesterol. Cholesterol is a membrane lipid whose
structure contains a steroid nucleus. It is the most
abundant type of steroid. Besides its membrane
functions, it also serves as a precursor for several
other types of lipids (Section 19.9).
Lipid bilayer. A lipid bilayer is the fundamental
structure associated with a cell membrane. It is a two-
layer structure of lipid molecules (mostly
phospholipids and glycolipids) in which the nonpolar
tails of the lipids are in the interior and the polar
heads are on the outside surfaces (Section 19.10).
Membrane transport mechanisms. The transport
mechanisms by which molecules enter and leave cells
include passive transport, facilitated transport, and
active transport. Passive and facilitated transport
follow a concentration gradient and do not involve
cellular energy expenditure. Active transport involves
movement against a concentration gradient and
requires the expenditure of cellular energy (Section
19.10).
Bile acids. Bile acids are cholesterol derivatives that
function as emsulsification lipids. They cause dietary
lipids to be soluble in the aqueous environment of the
digestive tract. Cholic acid and deoxycholic acids are
the major types of bile acids (Section 19.11).
Steroid hormones. Steroid hormones are cholesterol
derivatives that function as messenger lipids. The two
major types of steroid hormones are sex hormones
and adrenocorticoid hormones (Section 19.12).
Eicosanoids. Eicosanoids are fatty acid derivatives
that function as messenger lipids. The major classes
of eicosanoids are prostaglandins, thromboxanes, and
leukotrienes (Section 19.13).
Biological waxes. Biological waxes are protective-
coating lipids formed through the esterification of a
long-chain fatty acid to a long-chain alcohol (Section
19.14).
Saponifiable and nonsaponifiable lipids.
Saponifiable lipids are lipids that undergo hydrolysis
in basic solution to yield two or more smaller product
molecules. Nonsaponif able lipids are lipids that do
 BIOLOGICAL CHEMISTRY
not undergo hydrolysis in basic solution (Section
19.15).
Protein. A protein is a polymer in which the
monomer units are amino acids (Section 20.1).
Alpha-Amino acid. An alpha-amino acid is an
amino acid in which the amino group and the
carboxyl group are both attached to the alpha-carbon
atom (Section 20.2).
Standard amino acid. A standard amino acid is one
of the 20 alpha-amino acids that are normally present
in protein (Section 20.2).
Amino acid classifications. Amino acids are
classified as nonpolar, polar neutral, polar basic, or
polar acidic depending on the nature of the side chain
(R group) present (Section 20.2).
Essential amino acid. A standard amino acid needed
for protein synthesis that must be obtained from
dietary sources because the human body cannot
synthesize it in adequate amounts from other
substances (Section 20.3).
Chirality of amino acids. Amino acids found in
proteins are always left-handed (L isomer) (Section
20.4).
Zwitterion. A zwitterion is a molecule that has a
positive charge on one atom and a negative charge on
another atom. In neutral solution and in the solid
state, amino acids exist as zwitterions. For amino
acids in solution, the isoelectric point is the pH at
which the amino acid exists primarily in its
zwitterion form (Section 20.5).
Disulfide bond formation. The amino acid cysteine
readily dimerizes; the -SH groups of two cysteine
molecules interact to form a covalent disulfide bond
(Section 20.6).
Peptide bond. A peptide bond is an amide bond
involving the carboxyl group of one amino acid and
the amino group of another amino acid. In a protein,
the amino acids are linked to each other through
peptide bonds (Section 20.7).
Biochemically important peptides. Numerous small
peptides are biochemically active. Their functions
include hormonal action, neurotransmission
functions, and antioxidant activity (Section 20.8).
General characteristics of proteins. Proteins are
peptides with at least 40 amino acid residues. A
single peptide chain is present in a monomeric
protein, and two or more peptide chains are present in
a multimeric protein. A simple protein contains only
one or more peptide chains. A conjugated protein
contains one or more additional chemical
components, called prosthetic groups, in addition to
peptide chains (Section 20.9).
Primary protein structure. The primary structure of
a protein is the sequence of amino acids present in
the peptide chain or chains of the protein (Section
20.10).
Secondary protein structure. The secondary
structure of a protein is the arrangement in space of
the backbone portion of the protein. The two major
types of protein secondary structure are the alpha
helix and the beta pleated sheet (Section 20.11).
Tertiary protein structure. The tertiary structure of
a protein is the overall three-dimensional shape that
results from the attractive forces among amino acid
side chains (R groups) (Section 20.12).
Quaternary protein structure. The quaternary
structure of a protein involves the associations among
the peptide chains present in a multimeric protein
(Section 20.13).
Protein hydrolysis. Protein hydrolysis is a chemical
reaction in which peptide bonds within a protein are
broken through reaction with water. Complete
hydrolysis produces free amino acids (Section 20.14).
Protein denaturation. Protein denaturation is the
partial or complete disorganization of a protein’s
characteristic three-dimensional shape as a result of
disruption of its secondary, tertiary, and quaternary
structural interactions (Section 20.15).
Fibrous and globular proteins. Fibrous proteins are
generally insoluble in water and have a long, thin,
fibrous shape. Alpha Keratin and collagen are
important fibrous proteins. Globular proteins are
generally soluble in water and have a roughly
spherical or globular overall shape. Hemoglobin and
myoglobin are important globular proteins (Section
20.16).
Glycoproteins. Glycoproteins are conjugated
proteins that contain carbohydrates or carbohydrate
derivatives in addition to amino acids. Collagen and
immunoglobulins are important glycoproteins
(Section 20.18).
 BIOLOGICAL CHEMISTRY
Lipoproteins. Lipoproteins are conjugated proteins
that are composed of both lipids and amino acids.
Lipoproteins are classified on the basis of their
density (Section 20.19).
Enzymes. Enzymes are highly specialized protein
molecules that act as biochemical catalysts. Enzymes
have common names that provide information about
their function rather than their structure. The suffix -
ase is characteristic of most enzyme names (Section
21.1).
Enzyme structure. Simple enzymes are composed
only of protein (amino acids). Conjugated enzymes
have a nonprotein portion (cofactor) in addition to a
protein portion (apoenzyme). Cofactors may be small
organic molecules (coenzymes) or inorganic ions
(Section 21.2).
Enzyme classification. There are six classes of
enzymes based on function: oxidoreductases,
transferases, hydrolases, lyases, isomerases, and
ligases (Section 21.3).
Enzyme active site. An enzyme active site is the
relatively small part of the enzyme that is actually
involved in catalysis. It is where substrate binds to
the enzyme (Section 21.4).
Lock-and-key model of enzyme activity. The active
site in an enzyme has a fixed, rigid geometrical
conformation. Only substrates with a complementary
geometry can be accommodated at the active site
(Section 21.4).
Induced-f t model of enzyme activity. The active
site in an enzyme can undergo small changes in
geometry in order to accommodate a series of related
substrates (Section 21.4).
Enzyme activity. Enzyme activity is a measure of
the rate at which an enzyme converts substrate to
products. Four factors that affect enzyme activity are
temperature, pH, substrate concentration, and enzyme
concentration (Section 21.6).
Enzyme inhibition. An enzyme inhibitor slows or
stops the normal catalytic function of an enzyme by
binding to it. Three modes of inhibition are reversible
competitive inhibition, reversible noncompetitive
inhibition, and irreversible inhibition (Section 21.7).
Allosteric enzyme. An allosteric enzyme is an
enzyme with two or more protein chains and two
kinds of binding sites (for substrate and regulator)
(Section 21.8).
Zymogen. A zymogen is an inactive precursor of a
proteolytic enzyme; the zymogen is activated by a
chemical reaction that removes part of its structure
(Section 21.8).
Covalent modification. Covalent modification is a
cellular process for regulation of enzyme activity in
which the structure of an enzyme is modified through
formation of, or breaking of, a covalent bond. The
most commonly encountered type of covalent
modification involves a phosphate group being added
to, or removed from, an enzyme (Section 21.8).
Vitamins. A vitamin is an organic compound
necessary in small amounts for the normal growth of
humans and
some animals. Vitamins must be obtained from
dietary sources because they cannot be synthesized in
the body (Section 21.11).
Water-soluble vitamins. Vitamin C and the eight B
vitamins are the water-soluble vitamins. Vitamin C is
essential for the proper formation of bones and teeth
and is also an important antioxidant. All eight B
vitamins function as coenzymes (Section 21.12).
Fat-soluble vitamins. The four fat-soluble vitamins
are vitamins A, D, E, and K. The best-known
function of vitamin A is its role in vision. Vitamin D
is essential for the proper use of calcium and
phosphorus to form bones and teeth. The primary
function of vitamin E is as an antioxidant. Vitamin K
is essential in the regulation of blood clotting
(Section 21.13).
Nucleic acids. Nucleic acids are polymeric molecules
in which the repeating units are nucleotides. Cells
contain two kinds of nucleic acids—deoxyribonucleic
acids (DNA) and ribonucleic acids (RNA). The major
biochemical functions of DNA and RNA are,
respectively, transfer of genetic information and
synthesis of proteins (Section 22.1).
Nucleic acid building blocks. Three types of
subunits are present in a nucleic acid. They are: (1) a
pentose sugar (ribose or deoxyribose) (2) a nitrogen-
containing base (either a purine or pyrimidine
derivative) and (3) a phosphate group. The nitrogen-
containing bases are of five types: adenine (A),
guanine (G), cytosine (C), thymine (T), and uracil
(U) (Section 22.2).
 BIOLOGICAL CHEMISTRY
Nucleosides and nucleotides. A nucleoside is a
compound formed from a pentose sugar and a purine
or pyrimidine base derivative. A nucleotide is a
nucleoside to which a phosphate group has been
added (bonded to the sugar). Nucleotides are the
monomers for nucleic acid polymers (Section 22.3).
Primary nucleic acid structure. The “backbone” of
a nucleic acid molecule is a constant alternating
sequence of sugar and phosphate groups. Each sugar
unit has a nitrogen-containing base attached to it
(Section 22.4).
Complementary bases. Complementary bases are
specific pairs of bases in nucleic acid structures that
hydrogen-bond to each other (Section 22.5).
Secondary DNA structure. A DNA molecule exists
as two polynucleotide chains coiled around each
other in a double-helix arrangement. The double
helix is held together by hydrogen bonding between
complementary pairs of bases. Only two base-pairing
combinations occur: A with T, and C with G (Section
22.5).
DNA replication. DNA replication occurs when the
two strands of a parent DNA double helix separate
and act as templates for the synthesis of new chains
using the principle of complementary base pairing
(Section 22.6).
Chromosome. A chromosome is a structure that
consists of an individual DNA molecule bound to a
group of proteins (Section 22.6).
RNA molecules. Five important types of RNA
molecules, distinguished by their function, are
ribosomal RNA (rRNA), messenger RNA (mRNA),
heterogeneous nuclear RNA (hnRNA), transfer RNA
(tRNA), and small nuclear RNA (snRNA) (Section
22.8).
Transcription. Transcription is the process in which
the genetic information encoded in the base sequence
of DNA is copied into hnRNA/mRNA molecules
(Section 22.9).
Gene. A gene is a portion of a DNA molecule that
contains the base sequences needed for the
production of a specific hnRNA/mRNA molecule.
Genes are segmented, with portions called exons that
contain genetic information and portions called
introns that do not convey genetic information
(Section 22.9).
Codon. A codon is a three-nucleotide sequence in
mRNA that codes for a specific amino acid needed
during the process of protein synthesis (Section
22.10).
Genetic code. The genetic code consists of all the
mRNA codons that specify either a particular amino
acid or the termination of protein synthesis (Section
22.10).
Anticodon. An anticodon is a three-nucleotide
sequence in tRNA that binds to a complementary
sequence (a codon) in mRNA (Section 22.11).
Translation. Translation is the stage of protein
synthesis in which the codons in mRNA are
translated into amino acid sequences of new proteins.
Translation involves interactions between the codons
of mRNA and the anticodons of tRNA (Section
22.12).
Mutations. Mutations are changes in the base
sequence in DNA molecules (Section 22.13).
Recombinant DNA. Recombinant DNA molecules
are synthesized by splicing a segment of DNA,
usually a gene, from one organism into the DNA of
another organism (Section 22.15).
Polymerase chain reaction. The polymerase chain
reaction is a method for rapidly producing many
copies of a DNA sequence (Section 22.16)
Metabolism. Metabolism is the sum total of all the
biochemical reactions that take place in a living
organism. Metabolism consists of catabolism and
anabolism. Catabolic biochemical reactions involve
the breakdown of large molecules into smaller
fragments. Anabolic biochemical reactions synthesize
large molecules from smaller ones (Section 23.1).
Mitochondria. Mitochondria are membrane-
enclosed subcellular structures that are the site of
energy production in the form of ATP molecules.
Enzymes for both the citric acid cycle and the
electron transport chain are housed in the
mitochondria (Section 23.2).
Metabolic coenzymes. Three important coenzymes
involved in metabolic reactions are NAD+, FAD, and
CoA. NAD+ and FAD are oxidizing agents that
participate in the oxidation reactions of the citric acid
cycle. They transport hydrogen atoms and electrons
from the citric acid cycle to the electron transport
chain. CoA interacts with acetyl groups produced
 BIOLOGICAL CHEMISTRY
from food degradation to form acetyl CoA. Acetyl
CoA is the “fuel” for the citric acid cycle (Section
23.3).
Metabolic carboxylate ions. Five important
carboxylate ions involved as substrates in metabolic
reactions are malate, oxaloacetate, fumarate, alpha-
ketoglutarate, and citrate. The first three of these
carboxylate ions are polyfunctional derivatives of
succinic acid, the four-carbon dicarboxylic acid, and
the latter two are polyfunctional derivatives of
glutaric acid, the five-carbon dicarboxylic acid
(Section 23.4).
High-energy compounds. A high-energy compound
liberates a larger-than-normal amount of free energy
upon hydrolysis because structural features in the
molecule contribute to repulsive strain in one or more
bonds. Most high-energy biochemical molecules
contain phosphate groups (Section 23.5).
Common metabolic pathway. The common
metabolic pathway includes the reactions of the citric
acid cycle and those of the electron transport chain
and oxidative phosphorylation. The degradation
products from all types of foods (carbohydrates, fats,
and proteins) participate in the reactions of the
common
metabolic pathway (Section 23.6).
Citric acid cycle. The citric acid cycle is a cyclic
series of eight reactions that oxidize the acetyl
portion of acetyl CoA, resulting in the production of
two molecules of CO2. The complete oxidation of
one acetyl group produces three molecules of NADH,
one of FADH2, and one of GTP besides the CO2
(Section 23.7).
Electron transport chain. The electron transport
chain is a series of reactions that passes electrons
from NADH and FADH2 to molecular oxygen. Each
electron carrier that participates in the chain has an
increasing affinity for electrons. Upon accepting the
electrons and hydrogen ions, the O2 is reduced to
H2O (Section 23.8).
Oxidative phosphorylation. Oxidative
phosphorylation is the biochemical process by which
ATP is synthesized from ADP as the result of a
proton gradient across the inner mitochondrial
membrane. Oxidative phosphorylation is coupled to
the reactions of the electron transport chain (Section
23.9).
Chemiosmotic coupling. Chemiosmotic coupling
explains how the energy needed for ATP synthesis is
obtained. Synthesis takes place because of a flow of
protons across the inner mitochondrial membrane
(Section 23.10).
Importance of ATP. ATP is the link between energy
production and energy use in cells. The conversion of
ATP to ADP powers life processes, and the
conversion of ADP back to ATP regenerates the
energy expended in cell operation (Section 23.11).
Glycolysis. Glycolysis, a series of ten reactions that
occur in the cytosol, is a process in which one
glucose molecule is converted into two molecules of
pyruvate. A net gain of two molecules of ATP and
two molecules of NADH results from the
metabolizing of glucose to pyruvate (Section 24.2).
Fates of pyruvate. With respect to energy-yielding
metabolism, the pyruvate produced by glycolysis can
be converted to acetyl CoA under aerobic conditions
or to lactate under anaerobic conditions. Some
microorganisms convert pyruvate to ethanol, an
anaerobic process (Section 24.3).
Glycogenesis. Glycogenesis is the process whereby
excess glucose 6-phosphate is converted into
glycogen. The glycogen is stored in the liver and in
muscle tissue (Section 24.5).
Glycogenolysis. Glycogenolysis is the breakdown of
glycogen into glucose 6-phosphate. This process
occurs when muscles need energy and when the liver
is restoring a low blood-sugar level to normal
(Section 24.5).
Gluconeogenesis. Gluconeogenesis is the formation
of glucose from pyruvate, lactate, and certain other
substances. This process takes place in the liver when
glycogen supplies are being depleted and when
carbohydrate intake is low (Section 24.6).
Cori cycle. The Cori cycle is the cyclic process
involving the transport of lactate from muscle tissue
to the liver, the resynthesis of glucose by
gluconeogenesis, and the return of glucose to muscle
tissue (Section 24.6).
Pentose phosphate pathway. The pentose phosphate
pathway metabolizes glucose to produce ribose (a
pentose), NADPH, and other sugars needed for
biosynthesis (Section 24.8).
 BIOLOGICAL CHEMISTRY
Carbohydrate metabolism and hormones. Insulin
decreases blood-glucose levels by promoting the
uptake of glucose by cells. Glucagon increases blood-
glucose levels by promoting the conversion of
glycogen to glucose. Epinephrine stimulates the
release of glucose from glycogen in muscle cells
(Section 24.9)
Triacylglycerol digestion and absorption.
Triacylglycerols are digested (hydrolyzed) in the
intestine and then reassembled after passage into the
intestinal wall. Chylomicrons transport the
reassembled triacylglycerols from intestinal cells to
the bloodstream (Section 25.1).
Triacylglycerol storage and mobilization.
Triacylglycerols are stored as fat droplets in adipose
tissue. When they are needed for energy, enzyme-
controlled hydrolysis reactions liberate the fatty
acids, which then enter the bloodstream and travel to
tissues where they are utilized (Section 25.2).
Glycerol metabolism. Glycerol is first
phosphorylated and then oxidized to
dihydroxyacetone phosphate, a glycolysis pathway
intermediate. Through glycolysis and the common
metabolic pathway, the glycerol can be converted to
CO2 and H2O (Section 25.3).
Fatty acid degradation. Fatty acid degradation is
accomplished through the b-oxidation pathway. The
degradation process involves removal of carbon
atoms, two at a time, from the carboxyl end of the
fatty acid. There are four repeating reactions that
accompany the removal of each two-carbon unit. A
turn of the cycle also produces one molecule each of
acetyl CoA, NADH, and FADH2 (Section 25.4).
Ketone bodies. Acetoacetate, beta-hydroxybutyrate,
and acetone are known as ketone bodies. Synthesis
occurs mainly in the liver from acetyl CoA as a result
of excessive fatty acid degradation. During starvation
and in unchecked diabetes, the level of ketone bodies
in the blood becomes very high (Section 25.6).
Fatty acid biosynthesis. Fatty acid biosynthesis,
lipogenesis, occurs through the addition of two-
carbon units to a growing acyl chain. The added two-
carbon units come from malonyl CoA. A
multienzyme complex, an acyl carrier protein (ACP),
and NADPH are important parts of the biosynthetic
process (Section 25.7).
Biosynthesis of cholesterol. Cholesterol is
biosynthesized from acetyl CoA in a complex series
of reactions in which isoprene units are key
intermediates. Cholesterol is the precursor for the
various classes of steroid hormones (Section 25.9)
Protein digestion and absorption. Digestion of
proteins involves the hydrolysis of the peptide bonds
that link amino acids to each other. This process
begins in the stomach and is completed in the small
intestine. The amino acids released by digestion are
absorbed through the intestinal wall into the
bloodstream (Section 26.1).
Amino acid pool. The amino acid pool within cells
consists of varying amounts of each of the 20
standard amino acids found in proteins (Section
26.2).
Amino acid utilization. Amino acids from the amino
acid pool are used for protein synthesis, synthesis of
nonprotein nitrogen compounds, synthesis of
nonessential amino acids, and energy production
(Section 26.2).
Transamination. A transamination reaction is an
enzymecatalyzed transfer of an amino group from an
alpha-amino acid to an alpha-keto acid.
Transamination is a step in obtaining energy from
amino acids (Section 26.3).
Oxidative deamination. An oxidative deamination
reaction is a reaction in which an alpha-amino acid is
converted into an alpha-keto acid, accompanied by
the release of a free ammonium ion. Oxidative
deamination is a step in obtaining energy from amino
acids (Section 26.3).
Urea cycle. The urea cycle is the metabolic pathway
that converts ammonium ions and aspartate into urea.
This cycle processes the ammonium ions in the form
of carbamoyl phosphate, a compound formed from
CO2, NH4+, ATP, and H2O (Section 26.4).
Amino acid carbon skeletons. Amino acid carbon
skeletons (keto acids) are classified as glucogenic or
ketogenic on the basis of their catabolic pathways.
Glucogenic amino acids are degraded to
intermediates of the citric acid cycle and can be used
for glucose synthesis. Ketogenic amino acids are
degraded into acetoacetyl CoA or acetyl CoA and can
be used to make ketone bodies (Section 26.5).
 BIOLOGICAL CHEMISTRY
Amino acid biosynthesis. Amino acid biosynthesis
is the process in which the body synthesizes amino
acids from intermediates of the glycolysis pathway
and the citric acid cycle. Eleven amino acids can be
synthesized by the body. The other nine amino acids,
called essential amino acids, must be obtained from
the diet (Section 26.6).

Hemoglobin catabolism. Hemoglobin from red

blood cells undergoes a stepwise degradation to
biliverdin, to bilirubin, and then to bile pigments that
are excreted from the body (Section 26.7)