Biochemistry Flashcards
Midterms
the study of life processes, structures mechanism, reaction of the molecular levels
biochemistry
removal of carboxyl group of organic acids
decarboxylation
occurs when it gains oxygen or loses hydrogen
oxidation
addition of phosphate group
phosphorylation
takes place in the presence of oxygen
aerobic oxidation
reverse of oxidation
reduction
occurs in the absence of oxygen
anaerobic oxidation
defined as polyhydroxyaldehides or ketones or compound which produce them on hydrolysis
carbohydrates
addition of acyl group
acetylation
union of a substance with one or more water molecules
hydrolysis
simple fragments unite with one another to form a more complex compound
condensation
transfer of amino group
transamination
transfer of a methyl group
transmethylation
living matter is composed of mainly 6 elements
carbon, hydrogen, oxygen, nitrogen, phosphorus, sulfur
chemicals or molecules that are present in living organism
biomolecules
the most predominant and versatile element of life
carbon
french term of carbohydrates
hydrate de carbone
functions of carbohydrates
most abundant source of energy, storage of energy, cell growth and fertilization, protection layer for animal and plants
the compounds that have the same structural formula but differ in their spatial configuration
stereoisomers
the simplest group of carbohydrates and are often referred to as simple sugars
monosaccharides
an important character of monosaccharides
stereoisomerism
used to represent the stereoisomers that are not mirror images of one another
diastereomers
are a special type of stereoisomers that are mirror images of each other
enantiomers
meaning of d
Dextrorotatory
meaning of L
Levorotatory
the cyclic isomers differing from each other in configuration at anomeric carbon
anomers
defined as an atom in a molecule that is bonded to four different chemical species allowing for optical isomerism
chiral center
two sugars that differs in configuration at only 1 chiral center
epimers
it oxidizes glucose to gluconic acid
nitric acid
loosely defined group of molecules; water insoluble and soluble in organic solvents; hydrophobic; chief concentrated storage form of energy forming about 3.5% of the cell content
lipids
greek word of lipids
lipos-fat
reaction wherein the silver metal forms deposits and acts like a mirror; a qualitative test for glucoce
silver mirror test
lipids composed of what elements?
carbon, hydrogen, oxygen
follows the same mechanism as mentioned for the tollen’s reagent
fehling’s solution
building blocks of lipids
fatty acids, glycerol
double bonds joining the carbon atoms in the hydrocarbon tails
unsaturated
have just one carbon-carbon double bond
monounsaturated
functions of lipids
concentrated fuel reserve of the body, regulates the membrane permeability, source of fat soluble vitamins, cellular metabolic regulators, protect internal organs
these are carboxylic acids typically contain between 12 to 20 carbon atoms
fatty acids
have only single bonds joining the carbon atoms in their hydrocarbon tails
saturated fatty acids
simplest trihydric alcohol
glycerol
have two or more double bonds
polyunsaturated
able to pack closely together with one another, interacting with one another, interacting with one another through london force
hydrocarbon tails of saturated fatty acids
ester of fatty acids with alcohol
simple lipids
esters produced by combining fatty acids with long chain alcohols 14-16 carbon atoms
waxes
animals fats and vegetable oils are triglycerides
fats and oils
triglycerides composed of how many fatty acids?
3 fatty acids
double bonds can be broken to produce small organic molecules that have unpleasant odors
oxidation
made by combining glycerol, two fatty acids, one phosphate group and one alcohol molecule
glycerophospholipids
lipids that are composed of fatty acids, alcohol and an additional group, the prosthetic group
complex (compound) lipids
double bonds are removed by adding hydrogen with a presence of hydrogen
catalytic hydrogenation
the alcohol in this group of phospholipids
sphingosine
also known as soap making; hydrolysis of ester groups in the presence of OH-
saponification
obtained on the hydrolysis of group 1 and 2 lipids which possess the characteristics of lipids
derived lipids
contains a fatty acids, carbohydrate and nitrogenous base
glycolipids
macromolecular complexes of lipids with proteins
lipoproteins
long-chain lipids that are components of many biologically important pigments, such as chlorophyll and the visual pigment retinal ex: rubber
terpenes
found in membranes composed of four carbon rings
steroids
local hormones; tissue hormones
eicosanoids
gives rise to three major classes of eicosanoids; released on demand from the cell membrane
arachidonic acid
3 major classes of eicosanoids
prostaglandins. thromboxanes. leukotrienes
indicates that the enzyme cyclizes arachidonic acid that is it converts part of the molecules to a close-ring; incorporates oxygen into molecule
cyclooxygenase
catalyzes the reactions of arachidonic acid to leukotrienes A4
lipoxygenase
has a ketone on its ring
prostaglandin e2
functions of eicosanoids prostaglandins
mediator or pain, inducing fever, mucus protection, vasodilation (increased renal blood flow) in kidney, uterine contraction, motility
hydroxyl group and form a single bond to a carbon atom
prostaglandin f2
function of prostacyclin pgi2
vasodilation decreased platelet aggregation
functions of thromboxanes
vasoconstriction increased platelet aggregation
function of leukotrienes b4
chemotaxis
function of leukotrienes c4 and so on.,
eosinophils (bronchoconstriction
most abundant molecule in the living organism; makes up 50% of the dry weight of the cell
proteins
greek word or protein meaning holding the first place
proteios
in 1838 used the term proteins for the high molecular weight nitrogen rich and most abundant substances present in animals and plants
mulder
functions of proteins
movement, structure and support, cellular communication, digestion, transport or oxygen
suggested the name proteins to the group of organic compound
berzelius
5 major elements in proteins
carbon, hydrogen, oxygen, nitrogen, sulfur
group of organic compounds containing two functional groups amino acid and carboxyl
amino acids
most common amino acids
α-amino acids
the most common α-amino acids
L-α-amino acids
substances containing equal numbers of positive and negative charge-due to their carboxyl and amine group
zwitterions
contains a carboxyl group
polar acidic
side chain is alkyl an aromatic ring
non polar
usually an alcohol or a phenol
polar neutral
another name for amide bond
peptide bond
contains amino group
polar basic
between α-amino and v-carboxyl group
amide bond
the end of the peptide chain with the unreacted amino group
N-terminus
the end of the peptide chain with the free carboxyl group
C-terminus
made up of one or more polypeptide chain; can be classified as being either fibrous or globular
proteins
exists as long fibers or strings; usually tough and water insoluble, such as collagen and keratin
fibrous proteins
spherical in shape, highly folded and tend to be water soluble
globular proteins
type of proteins
fibrous, globular, membrane, disordered
some proteins contain chemical groups other than amino acids
conjugated proteins
functions of proteins additional
enzyme, transport, nutrient and storage, contractile and motile, structural, defense, regulatory
caused by disruption of the non covalent forces responsible for maintaining the native conformation
denaturation
factors that can caused denaturation
changes in temperature or pH, agitation, use of soaps or detergent
used to find out the amount of protein in biological fluids and foods
Kjeldahl’s method
molecule that reacts or can be an acid and base
ampotheric
give protein precipitate that turn flesh to red
millon’s test
alkaline solution of proteins will give rose pink to violet to purple color
biuret test
will give violet ring at the point of contact of the two solution
hopkin’s cole reaction
will give yellow to orange color when neutralized with NaOH
Xanthoproteic reaction
when solid protein is boiled in concentrated HCl with few drops of sucrose solution
Lieberman’s test
will produce black precipitate
test for the SH group
produce violet ring if glycoprotein is present
Molisch’s test
protein boiled with triketohydrindene hydrate
ninhydrin reaction
protein deficiency
kwashiorkor
simplest protein
glycine
coined the term catalysis (greek to dissolve)
berzelius
used the word enzyme (greek: yeast) to indicate the catalysis taking place in the biological systems
Kuhne
he named the active principle of zymase
Buchner
found contain a mixture of enzymes which could convert sugar to alcohol
zymase
first achieved the isolation and crystallization of the enzyme urease from jack bean and identified it as a protein
James sumner
defined as a substance that increases the velocity or rate of a chemical reaction
catalysts
biocatalyst; the catalyst of life; may be defined as biocatalysts synthesized by living cells
enzymes
addition or removal of water, ammonia, CO2
lyases
involved in oxidation-reduction reactions
oxidoreductases
hydrolysis of various compounds
hydrolases
synthetic reactions (greek: ligate- to bind) where two molecules are joined together and ATP is used
ligases
transfer of functional groups
transferases
isomerization reactions
isomerases
Factors affecting enzyme activity
concentration of enzymes, substrate, effect of temperature, pH, product concentration, activators, time, and light and radiation
the metal is not tightly held by the enzymes and be exchanged easily with other ions
metal-activated enzymes
these enzymes hold the metals rather than tightly which are not readily exchanged
metalloenzymes
optimum temperature for most of enzymes is between_____
35°C-40°C
inactivated enzyme
apoenzyme
coenzymes
cofactor
formula of holoenzyme
inactivated enzyme + coenzyme
fit together
lock and key hypothesis
prevent enzyme from bonding; blocking the active side
competitive inhibitor
changes shape to fit in the substrate: adjustment bind tightly
induced fit hypothesis
distort the shape; dumidikit sa enzyme
non-competitive inhibitor
