Biochemistry Flashcards
Midterms (132 cards)
1
Q
the study of life processes, structures mechanism, reaction of the molecular levels
A
biochemistry
2
Q
removal of carboxyl group of organic acids
A
decarboxylation
2
Q
occurs when it gains oxygen or loses hydrogen
A
oxidation
3
Q
addition of phosphate group
A
phosphorylation
3
Q
takes place in the presence of oxygen
A
aerobic oxidation
3
Q
reverse of oxidation
A
reduction
3
Q
occurs in the absence of oxygen
A
anaerobic oxidation
3
Q
defined as polyhydroxyaldehides or ketones or compound which produce them on hydrolysis
A
carbohydrates
3
Q
addition of acyl group
A
acetylation
3
Q
union of a substance with one or more water molecules
A
hydrolysis
3
Q
simple fragments unite with one another to form a more complex compound
A
condensation
3
Q
transfer of amino group
A
transamination
3
Q
transfer of a methyl group
A
transmethylation
3
Q
living matter is composed of mainly 6 elements
A
carbon, hydrogen, oxygen, nitrogen, phosphorus, sulfur
3
Q
chemicals or molecules that are present in living organism
A
biomolecules
4
Q
the most predominant and versatile element of life
A
carbon
4
Q
french term of carbohydrates
A
hydrate de carbone
4
Q
functions of carbohydrates
A
most abundant source of energy, storage of energy, cell growth and fertilization, protection layer for animal and plants
5
Q
the compounds that have the same structural formula but differ in their spatial configuration
A
stereoisomers
5
Q
the simplest group of carbohydrates and are often referred to as simple sugars
A
monosaccharides
5
Q
an important character of monosaccharides
A
stereoisomerism
6
Q
used to represent the stereoisomers that are not mirror images of one another
A
diastereomers
6
Q
are a special type of stereoisomers that are mirror images of each other
A
enantiomers
7
Q
meaning of d
A
Dextrorotatory
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meaning of L
Levorotatory
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the cyclic isomers differing from each other in configuration at anomeric carbon
anomers
8
defined as an atom in a molecule that is bonded to four different chemical species allowing for optical isomerism
chiral center
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two sugars that differs in configuration at only 1 chiral center
epimers
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it oxidizes glucose to gluconic acid
nitric acid
9
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
9
greek word of lipids
lipos-fat
9
reaction wherein the silver metal forms deposits and acts like a mirror; a qualitative test for glucoce
silver mirror test
10
lipids composed of what elements?
carbon, hydrogen, oxygen
10
follows the same mechanism as mentioned for the tollen's reagent
fehling's solution
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building blocks of lipids
fatty acids, glycerol
10
double bonds joining the carbon atoms in the hydrocarbon tails
unsaturated
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have just one carbon-carbon double bond
monounsaturated
10
functions of lipids
concentrated fuel reserve of the body, regulates the membrane permeability, source of fat soluble vitamins, cellular metabolic regulators, protect internal organs
10
these are carboxylic acids typically contain between 12 to 20 carbon atoms
fatty acids
10
have only single bonds joining the carbon atoms in their hydrocarbon tails
saturated fatty acids
10
simplest trihydric alcohol
glycerol
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have two or more double bonds
polyunsaturated
10
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
11
ester of fatty acids with alcohol
simple lipids
11
esters produced by combining fatty acids with long chain alcohols 14-16 carbon atoms
waxes
11
animals fats and vegetable oils are triglycerides
fats and oils
12
triglycerides composed of how many fatty acids?
3 fatty acids
12
double bonds can be broken to produce small organic molecules that have unpleasant odors
oxidation
13
made by combining glycerol, two fatty acids, one phosphate group and one alcohol molecule
glycerophospholipids
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lipids that are composed of fatty acids, alcohol and an additional group, the prosthetic group
complex (compound) lipids
13
double bonds are removed by adding hydrogen with a presence of hydrogen
catalytic hydrogenation
13
the alcohol in this group of phospholipids
sphingosine
13
also known as soap making; hydrolysis of ester groups in the presence of OH-
saponification
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obtained on the hydrolysis of group 1 and 2 lipids which possess the characteristics of lipids
derived lipids
14
contains a fatty acids, carbohydrate and nitrogenous base
glycolipids
14
macromolecular complexes of lipids with proteins
lipoproteins
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long-chain lipids that are components of many biologically important pigments, such as chlorophyll and the visual pigment retinal ex: rubber
terpenes
14
found in membranes composed of four carbon rings
steroids
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local hormones; tissue hormones
eicosanoids
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gives rise to three major classes of eicosanoids; released on demand from the cell membrane
arachidonic acid
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3 major classes of eicosanoids
prostaglandins. thromboxanes. leukotrienes
17
indicates that the enzyme cyclizes arachidonic acid that is it converts part of the molecules to a close-ring; incorporates oxygen into molecule
cyclooxygenase
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catalyzes the reactions of arachidonic acid to leukotrienes A4
lipoxygenase
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has a ketone on its ring
prostaglandin e2
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functions of eicosanoids prostaglandins
mediator or pain, inducing fever, mucus protection, vasodilation (increased renal blood flow) in kidney, uterine contraction, motility
19
hydroxyl group and form a single bond to a carbon atom
prostaglandin f2
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function of prostacyclin pgi2
vasodilation decreased platelet aggregation
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functions of thromboxanes
vasoconstriction increased platelet aggregation
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function of leukotrienes b4
chemotaxis
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function of leukotrienes c4 and so on.,
eosinophils (bronchoconstriction
21
most abundant molecule in the living organism; makes up 50% of the dry weight of the cell
proteins
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greek word or protein meaning holding the first place
proteios
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in 1838 used the term proteins for the high molecular weight nitrogen rich and most abundant substances present in animals and plants
mulder
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functions of proteins
movement, structure and support, cellular communication, digestion, transport or oxygen
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suggested the name proteins to the group of organic compound
berzelius
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5 major elements in proteins
carbon, hydrogen, oxygen, nitrogen, sulfur
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group of organic compounds containing two functional groups amino acid and carboxyl
amino acids
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most common amino acids
α-amino acids
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the most common α-amino acids
L-α-amino acids
24
substances containing equal numbers of positive and negative charge-due to their carboxyl and amine group
zwitterions
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contains a carboxyl group
polar acidic
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side chain is alkyl an aromatic ring
non polar
25
usually an alcohol or a phenol
polar neutral
25
another name for amide bond
peptide bond
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contains amino group
polar basic
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between α-amino and v-carboxyl group
amide bond
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the end of the peptide chain with the unreacted amino group
N-terminus
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the end of the peptide chain with the free carboxyl group
C-terminus
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made up of one or more polypeptide chain; can be classified as being either fibrous or globular
proteins
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exists as long fibers or strings; usually tough and water insoluble, such as collagen and keratin
fibrous proteins
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spherical in shape, highly folded and tend to be water soluble
globular proteins
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type of proteins
fibrous, globular, membrane, disordered
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some proteins contain chemical groups other than amino acids
conjugated proteins
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functions of proteins additional
enzyme, transport, nutrient and storage, contractile and motile, structural, defense, regulatory
26
caused by disruption of the non covalent forces responsible for maintaining the native conformation
denaturation
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factors that can caused denaturation
changes in temperature or pH, agitation, use of soaps or detergent
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used to find out the amount of protein in biological fluids and foods
Kjeldahl's method
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molecule that reacts or can be an acid and base
ampotheric
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give protein precipitate that turn flesh to red
millon's test
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alkaline solution of proteins will give rose pink to violet to purple color
biuret test
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will give violet ring at the point of contact of the two solution
hopkin's cole reaction
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will give yellow to orange color when neutralized with NaOH
Xanthoproteic reaction
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when solid protein is boiled in concentrated HCl with few drops of sucrose solution
Lieberman's test
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will produce black precipitate
test for the SH group
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produce violet ring if glycoprotein is present
Molisch's test
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protein boiled with triketohydrindene hydrate
ninhydrin reaction
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protein deficiency
kwashiorkor
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simplest protein
glycine
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coined the term catalysis (greek to dissolve)
berzelius
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used the word enzyme (greek: yeast) to indicate the catalysis taking place in the biological systems
Kuhne
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he named the active principle of zymase
Buchner
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found contain a mixture of enzymes which could convert sugar to alcohol
zymase
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first achieved the isolation and crystallization of the enzyme urease from jack bean and identified it as a protein
James sumner
37
defined as a substance that increases the velocity or rate of a chemical reaction
catalysts
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biocatalyst; the catalyst of life; may be defined as biocatalysts synthesized by living cells
enzymes
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addition or removal of water, ammonia, CO2
lyases
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involved in oxidation-reduction reactions
oxidoreductases
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hydrolysis of various compounds
hydrolases
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synthetic reactions (greek: ligate- to bind) where two molecules are joined together and ATP is used
ligases
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transfer of functional groups
transferases
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isomerization reactions
isomerases
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Factors affecting enzyme activity
concentration of enzymes, substrate, effect of temperature, pH, product concentration, activators, time, and light and radiation
41
the metal is not tightly held by the enzymes and be exchanged easily with other ions
metal-activated enzymes
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these enzymes hold the metals rather than tightly which are not readily exchanged
metalloenzymes
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optimum temperature for most of enzymes is between_____
35°C-40°C
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inactivated enzyme
apoenzyme
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coenzymes
cofactor
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formula of holoenzyme
inactivated enzyme + coenzyme
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fit together
lock and key hypothesis
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prevent enzyme from bonding; blocking the active side
competitive inhibitor
45
changes shape to fit in the substrate: adjustment bind tightly
induced fit hypothesis
46
distort the shape; dumidikit sa enzyme
non-competitive inhibitor
