genbio 1st exam 2nd qrtr

lipids, nucleic acids, carbohydrates, and proteins

4 types of biomolecules

diglycerides and triglycerides

polymers of lipids

glycerol and fatty acids

monomers of lipids

dna and rna

polymers of nucleic acids

nucleotides

monomers of nucleic acids

polysaccharides and disaccharides

polymers of carbohydrates

monosaccharides

monomers of carbohydrates

polypeptides

polymers of proteins

amino acids

monomers of proteins

carbohydrates

organic molecules that serve as a primary source of energy for living organisms and play essential structural and functional roles,

C,H,O (1:2:1 ratio)

elements present in carbohydrates

monosaccharides

one-molecule sugars

disaccharides

two monosaccharides linked together

polysaccharides

more than 10 monosaccharides linked together

starch, glycogen, cellulose, and chitin

4 types of polysaccharides

starch

used for energy storage in plants and they provide a quick form of energy for the body

glycogen

formed in the liver and used for energy storage in animals

cellulose

provides structural support in plants (found in the cell wall)

chitin

found in exoskeleton and arthropods (insects, spiders) and found in cell wall of some fungi

lipids

Store energy, Insulates your body, and make up the cell membrane. these are Hydrophobic (water-fearing) and do not dissolve in water.

C,H,O

elements present in lipid

saturated and unsaturated

2 types of lipids

saturated

The bonds between all the carbons are single bonds.

Solid at room temperature

Mainly animal fats (bacon grease, lard)

unsaturated

There is at least one double or triple bond between carbons present.

Liquid at room temperature

Mainly plant based fats (olive oil) as well as oily fish (Tuna, Sardines)

proteins

Transport molecules in and out of the cell

Control the speed of chemical reactions

Used for growth and repair

C,H,O,N

elements present in proteins

glycine (G)

amino acid Gly

Alanine (A)

amino acid Ala

leucine (L)

amino acid leu

methionine (M)

amino acid met

phenylalanine (F)

amino acid phe

tryptophan (W)

amino acid trp

lysine (K)

amino acid lys

glutamine (Q)

amino acid gln

serine (S)

amino acid ser

proline (P)

amino acid pro

valine (V)

amino acid val

isoleucine (I)

amino acid ile

cysteine (C)

amino acid cys

tyrosine (Y)

amino acid tyr

histidine (H)

amino acid his

arginine (N)

amino acid arg

aspartic acid (D)

amino acid asp

threonine (T)

amino acid thr

nucleic acids

Holds the instructions to make proteins.

Provide our genetic information

C,H,O,N,P

elements present in nucleic acids

enzymes

are protein macromolecules. They have a defined amino acid sequence, and are typically 100-500 amino acids long. They have a defined three-dimensional structure. they also act as a catalyst to a chemical or biochemical reaction, with a defined mechanism. it is also reusable.

Oxidoreductase

an enzyme that catalyzes the transfer of electrons from one molecule

dehydrogenases, oxidases, peroxidases, and reductases

4 types of enzymes

Oxidoreductase, transferases, hydrolases, lyases, isomerase, and ligases

6 Enzymes based upon the class of organic chemical reaction catalyzed:

transferases

Catalyze group transfer reactions; often require coenzymes

Hydrolases

Enzymes that bring about hydrolysis of various compounds.

Lyases

catalyzed the addition or removal of functional group to form a double bond. enzymes specialized in the break or splitting of bonds in a process other than hydrolysis

isomerase

enzymes involved in isomerization reactions. intermolecular group transfer

ligases

enzymes catalyzing the synthetic two molecules joined together and ATP is used.

apoenzyme, haloenzyme, cofactor, and coenzyme

4 enzyme components

apoenzyme

It is an inactive enzyme, which activation occurs upon binding of an organic or inorganic cofactor. This enzyme is a protein that lack its necessary cofactor(s) for proper functioning

haloenzyme

are the active forms of apoenzymes, (Apoenzyme plus cofactor)

cofactor

is mostly a metallic ion that is required for an enzyme’s activity. _____ can be considered "helper molecules" that assist in biochemical transformations.

coenzyme

are non-protein organic molecules that are mostly derivatives of vitamins soluble in water by phosphorylation. Examples are organic cofactor (e.g., NADH, FADH)

lock and key hypothesis

It was suggested by Arrhenius that the shape of the Active Sites of Enzymes is exactly Complementary to the shape of the Substrate.

induced-fit model

A more recent model suggested by Daniel Koshland the _________. It states that the shape of Active Sites are not exactly Complementary, but are changed according to the substrate molecules.

temperature, ph, enzyme concentration, and substrate concentration

4 Factors affecting the rate of enzyme actions

temperature

Extreme __________ can cause an enzymes to lose it shape (denature) and stop working. the optimal ______ of this is 35 degrees to 40 degrees celsius.

ph (power of hydrogen)

For most enzymes this is about pH 7-8 but a few enzymes can work at extreme pH, such as protease enzymes in animal stomachs, which have an optimum of pH 1. Enzymes have an optimum ___________ at which they work fastest (ph 4-6).

enzyme concentration

As the __________ increases the rate of the reaction increases linearly. At very ___________ concentration the substrate concentration may become rate-limiting.

substrate concentration

As the ___________ increases, the rate increases because more substrate molecules can collide with enzyme molecules, so more reactions will take place.

competitive inhibitors, non-competitive inhibitors, and uncompetitive inhibitors

3 types of enzyme inhibitors (inhibition)

competitive inhibitors

A molecule similar in structure to a substrate can bind to an enzyme’s active site and compete with substrate

non-competitive inhibitors

attach to the enzyme at an allosteric site, which is a site other than the active site distort the tertiary protein structure and alter the shape of the active site.

oxidation-reduction (redox)

a type of chemical reaction that involves a transfer of electrons between two species. All _______ reactions involve the transfer of electrons from one atom to another

Glycine (G), Alanine (A), Leucine (L), Methionine (M), Phenylalanine (P), Tryptophan (W), Lysine (K), Glutamine (Q), Glutamic Acid (E), Serine (S), Proline (P), Valine (V), Isoleucine (I), Cysteine (C), Tyrosine (Y), Histidine (H), Arginine (R), Asparagine (N), Aspartic Acid (D), Threonine (T)

20 amino acids and their letter