Biochem Flashcards
helps in the conversion of energy to ATP
Thiamin (B1)
for energy production, cellular function and metabolism
riboflavin (B2)
helps in energy conversiin and creatiin and repair of DNA
niacin (B3)
used to make coenzyme A, for breakdown of fatty acids
pantothenic acid (B5)
maintain proper levels of the amino acid homocysteine
pyridoxine (B6)
for healthy hair, skin, nails
biotin (B7)
for pregnancy
folate and folic acid (B9)
helps form red blood cells and DNA
Cobalamin (B12)
inactive enzyme found in the stomach
pepsinogen
cannot be made by the body; must be from the food
essential amino acid
bodies can produce
non essential amino acids
food that can supple all nine essential amino acids
complete proteins
do not contain adequate anounts of one or more essential amino acids
incomplete proteins
first step in breaking down food proteins
transamination
glutamate loses its amino acid, forming ammonium and reforming a ketoglutarate
oxidtive deamination
building block of proteins
amino acids
required in the human diet and nit synthesized by the body
essential
type of structure where most carbonyl grouos of peptide bonds forms a hydrogen bond with the amide nitrogen of another peptide bond
alpha helix
when the amino acid alanine added to a solution with a ph 7.3, it becomes
an anion
increasing the solubility of a protein in solution by adding ions
salting in
local spatial arrangement of a polypeptide backbone atoms without regard to the conformation of its side chain
secondary structure
more likely to found in a proteins interior away from aqueous solvent molecules (hydrophobic; nonpolar amino acid)
Val, Leu, Ile, Met, Phe
most likely to reside in the membrane-anchoring domain of a membrane protein
isoleucine, valine, ohenylalanine
primry stabilizing force of a protein secondary structure
hydrogen bonds
two types of b-pleated sheets
prallel and antiparallel
protein that have a specific chemical structure and function
domains
quaternary structure of a proteins
intertwining of two or more polypeptide
hemoglobin
4 polypeptide chains: 2 a chains and 2 b chains
action of disrupting the 3D shape of protein
denaturation
least afftected in protein denaturation
primary structure
imino acid froound in the protein structure
proline
bonds in the protein structure that are not broken on denaturation
peptide bonds
nature of the peptide bond
a partial double bond
function of enzyme
catalysts
conjugated enzyme
apoenzyme
enzyme cofactors that bind covalently at the active site of an enzyme
prodthetic grouos
an enzyme active site is the location in an enzyme where substrate molecules
undergo change
optimal temperature range for the majority of enzymes
35-40C
reactants of an enzyme catalyzed reaction
substrates
where binding occurs
active site
enzyme catalyzes reactions by
decreasing the free energy of activation
apoenzyme
without cofactors
NAD+, FAD and FMN are all cofactors for
oxidireductases
rate of second order rxn depends on
two substrate
site of amino acid catabolism
liver
first step in catabolism of amino acids
removal of amino group
true about urea
the primary ni trogenous waste products of humans
a glucogenic amino acids is one which is degraded to
pyruvate or citric acid cycle internediates
transamination
a-amino group is removed fron the amino acid
transamination is the transfer of an amino
group from n amino acid to a keto acid
rate determining step of michaelic menten kinetics
the complex dissociation step to produce product
competitive inhibitor of an enzyme works by
fitting into the enzymes active site of an
if n enzyne is described by the michaelis menten, a conpetitive inhibitor will
increase the Km but not change the vmax
binds to an enzyme at its active site
reversible competitive inhibitor
competitive inhibitor of enzyme
structurally similar to the substrate
uncompetitive inhibitor binds to
ES
reversible inhibitor that can bind to either E alone
non competitive inhibitor
in lineweaver burk plot, conpetitive inhibitor shows
it changes the x intercept
non competitive inhibitor of an enzyme catalyzed reaction
decreases vmax, binds to ES
classical uncompetitive inhibitor is a compound that binds
reversibly to the enzyme substrate complex yielding an inactive ESI complex
some enzymatic regulatiin is allosteric
an enzyme with more than one subunit
glucose + fructose
sucrose
galactose + glucose
lactose
glucose + glucose
maltose
glucose and fructose are examples of of
single sugars
not a polysaccharide
sucrose
more complex sugar
starches
what does insulin do
inhibit gluconeogenesis and stimulate glycolysis
describe the flow of genetic information ithin biological system
central dogma
three structutal subunits of each nucleotides
sugar, heterocyclic base, phosphodiester
nucleotides
nucleoside + phospate
major energy curency of the cell
ATP
guanine
cytosine
adenosine
thymine
dna coils around a core of proteins
histones
DNA + histones
nucleosome
nit considered a pyrimidine
guanine
base present only in RNA
uracil
role of hydrogen bond in the structure of DNA
connect base pairs
whise xray work aided watson and crick in discovery of double helix
R. Franklin
fragments move most quickly through a gel
small fragments
nucleotide bases and aromatic amino acids absorb light at
260 and 280 nm
found in RNA but not DNA
uracil
true about pairing bases in DNA
purines always pair with pyrimidines
both strands of dna serve aa templates concurrently in
replication
repairs nicked DNA
dna ligase
replication of chrimosmes by eukaryotes occurs in relatively short period of time because
each chromosme contain multiple replicons
DNA molecule is precisely synthesized
replication
enzymes adds complementary bases during replication
polymerase
enzymes unwind short stretches of DNA helix immediately ahead of replication fork
helicases
dna plymerase removes RNA primers in DNA synthesis
polymerase I
dna replication takes place in which direction
5’ to 3’
enzyme responsible for proofreading base pairing
dna polymerase
5’ and 3’ related to the
carbon number in sugar
main damaging effect of UV radiation on DNA
formation kf thymine dimers
enzyme used for synthesis of RNA under direction of DNA
RNA polymerase
product of transcription
mRNA
RNA bind to amino acid
tRNA
recognition/binding site of RNA polymerase
promoter
mrna transcript of gene contains
start codon, stop codon, terminator
where DNA transcribed into mRNA
nucleus
site of protein synthesis
ribosome
indicate an active site for protein synthesis
polysomr
not necessary for protein synthesis to occur once transcription is completed
DNA
during process of translation
peptide is passed from trna in the P site to A site
nucleolus of the nucleus is the site where
rRNA is transcribed and ribosomal subunits are assembled
ribosome are composed of
proteins and RNA
required for protein synthesis
trna, mrna, rrna
mRNA binds
to the small subunit
ribosomes select the correct tRNAs
solely on the basis of their anticodons
amino acids starts all proteins synthesis
methionine
macromolecules that does not dissolve in water
lipids
monomers of lipids
fatty acids and glycerol
lipids function except
enzyme action
fats that have fatty acids with only single covalent bonds in their carbon skeleton
saturated
polymer
nucleic acid
higher melting point
triglyceride containing only stearic acid and glycerol
hydrolysis of a triglycerides
fatty acids and glycerol
important function of cholesterol
modulate membrane fluidity
fat soluble vitamin that regulates blood clot
vit K
breaking down of molecules
catabolism
building up of molecules
anabolism
release of energy from glucose compled to ATP synthesis
cellular respiration
atp phosphate bond has _ energy
7.3 kcal energy
cellular respiration takes place
mitochondria
glycolytic pathway regulation involves
allosteric stimulation by adp
allosteric inhibitiin by atp
feedback inhibitiin by atp
glycolysis occur
cytoplasm
released energy obtained by oxidation of glucose stored as
atp
enzymes of glycolysis located in
cytosol
atp is from which general category of molecules
nucleotides
regulates glycolysis steps
phosphofructokinase, hexose kinase, pyruvate kinase
not a mechanism for altering the flux of metabolites
block active sites
phophofructokinase is inhibited and activated by
atp and adp
biological redox rxn involves
oxidizing agent, gain of electrons, teducing agent
coenzyme Q involved jn electron transport as
a lipid soluble electron carrier
FAD is reduced FADH2 during
Krebs cycle
during glycolysis, electrons removed from glucose are passed to
NAD
co2 is primary product of
krebs cycle
not oresent during the TCA cycle
O2
correct order of stages
glycolysis, pyrivated oxidation, citric acid cycle, oxidative phophorylation
products of citric acid cycle
NADH, ATP, FADH2 and CO2
krebs cycle begins when pyruvic acid produced by glycolysisi enters
mitochondrion
the NADH produced by glycolysis ultimately donates its high energy electrons to
electron transport chains in mitochondiria
main purpose of transport chains
convert adp to atp
oxidative phosphorylation requires
electron transport system
proteins of electron transport chains located
mitochondrial inner membrane
atp synthase for most atp synthesis in the body located
inner side of the inner mitochondria membrane
final electron acceptor
oxygen
functioning anaerobically
lactate
glucagon activate what
gluconeogenisis and glycogenolysis
not a way of producing ATP in humans
alcohol fermentation
aerobic product of pyruvate catabolic metabolism
acetyl CoA
TCA cyle
controlled by the ADP/ATP ratio and the NADH concentration
hormonal levels is true
after running 20miles, epinephrine and glucagon are high and insulin is low
considered umeukryotes
archaea
spherical bactera
coccus
organism completely dependent on atmospheric oxygen for growth
obligate aerobe
organism grows best above 50C
thermophilic
food preservation by using salts and sugars works by
creating hypertonic environment
using microbes to clean
bioremediation
mucus helps in protecting against pathogens by
restricting access to mucosal surfaces
production of citric acid
aspergillus niger
starvation proteins
stationary phase
period between inoculation of bacteria in a culture medium and beginning of multiplcation
lag phase
batch fed, substrate is added how
periodically throughout the fermentation
