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biochem_keubel > quiz 7--nitrogen structures/8-enzymes > Flashcards

quiz 7--nitrogen structures/8-enzymes Flashcards

1
Q

What are amino acids?

A

Amines the build protiens. They are the subunits/monomers of proteins

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2
Q

What are porphyrins?

A

They are nitrogen containing ring structures that chelate a metal ion in the center of the ring, specilaized to hold the ion in place without bonding it.
-complex heterocyclic amine molecules with important roles in enzymes and enzyme-related processes.

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3
Q

What are nucleotides?

A

Monomers for nuclei acids. provide information storage and processing molecules for creating genetic material — the primary genetic materials are DNA and several types of RNA.

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4
Q

“R”

A

any aliphatic or aromatic group and

makes the amino acid unique

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5
Q

A single amino acid

A

monopeptide

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6
Q

What does a polypeptide become once it develops its secondary and tertiary structure by folding

A

a protein.

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7
Q

what joins two amino acids?

A

An amide or peptide bond. Therfore proteins are amides.

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8
Q

How is the amide or peptide bond formed?

A

by dehydration synthesis

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9
Q

what does a ribosome make a polypeptide?

A

a primary structure

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10
Q

Glutathione

A

An important tripeptide. a cell’s major

antioxidant molecule. It is composed of glutamic acid, cysteine and glycine — 3 amino acids.

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11
Q

thiol (sulfhydryl) group

A

SH – is the active oxidant scavenger.

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12
Q

20 specific amino acids

A

Humans have the genetic code/enzymes to
synthesize 12 of these, but needs to acquire 8 of
these from food protein — and these 8 are properly called essential amino acids.

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13
Q

test question: which amino acids in animals are incorporated into proteins?

A

only the L- form enantiomer amino acids and only α- chiral amino acids are incorporated into proteins

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14
Q

test question: What forms do enzymes may or may not convert?

A

the D- and β- forms to L- and α- forms for utilization in protein synthesis. Therefore, the L- α form of an amino acid is the only conformation
incorporated into proteins.

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15
Q

Sulfur-containing aminos

A

cysteine and methionine are important in protein folding and integrity by forming disulfide bridges

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16
Q

Charged or uncharged molecules

A

net charge on aminos can be negative, neutral, or positive — this causes attraction and repulsion when the polypeptide folds into a protein.

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17
Q

actin, myosin

A

two major proteins in muscles. movement, tendon muscle.

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18
Q

Protein roles

A

Enzymes — catalyze a myriad of biochemical
processes
– Structural proteins — connective tissue, skin, collagen
– Movement — tendon, muscle (actin, myosin)
– Messengers/hormomes/regulatory molecules —
especially in metabolism regulation (insulin, glucagon)
– Transport — provide product transport in the blood (hemoglobin); plasmalemma transport and channel proteins
– Defense — immunoglobulins, or B-cell mediated
(humoral) immunity
– Nutrient storage — milk protein, albumin

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19
Q

4 types of actions that make proteins

A

-A polypeptide produced by a ribosome is a linear, unfolded chain of amino acids linked with peptide bonds. This is a primary structure (or conformation) (1°) of the protein.
-secondary structure (2°) forms as hydrogen
bonding between specific amino units begins the folding process.
-tertiary structure (3°) folds the polypeptide even further, as disulfide bonds, charge attractions/ repulsions, and hydrophobic/hydrophilic attractions are lined up. Most proteins are complete at this stage.
-Quaternary structures (4°) are created when 2 or
more tertiary proteins form similar weak bonds between each other, creating often massive, multi-protein molecules. Hemoglobin in blood is one such quaternary structure. Immunoglobulins (antibodies) are another.

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20
Q

What is an enzyme?

A

a cataylst

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21
Q

what is an active site?

A

sites within the macromolecule where the catalytic work of the enzyme takes place — a cavity in the enzyme where the desired reaction takes place.
-Splitting or joining molecules and flipping conformation occur in active sites.

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22
Q

sustrates?

A

molecules that will be acted upon by the enzyme.

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23
Q

what is the characteristic element in Porphyrin?

A

cobalt

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24
Q

what chain do nucleotides form?

A

a chain composed of a phosphate-sugar backbone of either ribose or deoxyribose sugars and phosphate (PO4)
-Nucleotides themselves are complex molecules
composed of 3 subunits — a nitrogenous base, a
sugar, and a phosphate group

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25
Q

what are the 3 parts to a nucleotide?

A
  1. ) a nitrogenous base of 2 types: either a purine(2 rings) or pyrimidine (1 ring)
  2. ) with a monosaccharide (simple sugar—ribose or deoxyribose )
  3. ) a phosphate group
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26
Q

xanthines

A

form some very common molecules in nature such as plant pigments and caffeine

27
Q

what completes the formation of nucleotides from nucleosides?

A

Phosphorylation of nucleosides by bonding a

phosphate group.

28
Q

Adenosine

A

is used as a base for some of the most important molecules in the cell — ATP (adenosine triphosphate), NADH, and cAMP (cyclic adenosine
monophosphate).

29
Q

DNA

A

Adenine
Guanine
Cytosine
Thymine

30
Q

RNA

A

Adenine
Guanine
Cytosine
Uracil

31
Q

DNA

A

Adenine with Thymine
Thymine with Adenine
Cytosine with Guanine
Guanine with Cytosine

32
Q

RNA

A

Adenine with Uracil
Uracil with Adenine
Cytosine with Guanine
Guanine with Cytosine

33
Q

what is the function of DNA?

A

a storage molecule for genetic data

34
Q

types of RNA

A

rRNA – ribosomal RNA (hydrogen bonded)
tRNA – transfer RNA (hydrogen bonded)
mRNA – messenger RNA (open unbonded)

35
Q

what does (messenger) mRNA do?

A

carries the protein code from the nucleus to the cell’s manufactories as information packets called codons.

36
Q

(Transfer) tRNA

A

carry amino acids into the protein synthesis process in the ribosome. There are twenty different tRNAs which code for each of the 20 amino acids used in human protein.

37
Q

Catalysts

A

work to lower the activation energy of chemical reactions

38
Q

reaction rate

A

greatly accelerated

39
Q

Substrate

A

generic name for a molecule that will be worked on by an enzyme

40
Q

Enzyme activity is affected by many external

factors

A

– Presence or absence of substrates
– pH changes or other ionic factors
– Temperature range
– Availability of nutrients: ATP, cofactors, coenzymes, and ions
– The functionality of the enzyme — is it damaged
and not yet replaced?
– Molecules may be present causing competitive
inhibition of the active site — drugs, herbs,
toxins, organisms

41
Q

Enzymes are typically classified by the chemical nature of the reactions they catalyze. “ase” always indicates an enzyme

A

– Oxidoreductases – remove molecules or atoms from substrates
– Transferases – transfer functional groups from one molecule to another, such as moving a phosphate group
– Hydrolases – add water to substrates
– Lyases – work with double bonds
– Isomerases – change the isomeric status of a molecule
– Ligases – join or release carbon bonds and requires ATP

42
Q

what is an enzyme cascade?

A

a number of enzymes work on substrates in a specific order — an orderly chain of events facilitated by different enzymes.
For example, glycolysis is a typical enzyme cascade.

43
Q

what are enzymes are dependent for proper function?

A

several non-protein molecules called cofactors

44
Q

apoenzyme

A

When an enzyme does not have its cofactors present, and is not functional

45
Q

holoenzyme.

A

An enzyme with cofactors and fully functioning

46
Q

Cofactors

A

A cofactor is a non-protein molecule that has

either a tight or loose affinity to an enzyme and is required for enzymatic action.

47
Q

what are the two types of cofactors?

A

prosthetic groups and coenzymes

48
Q

what coenzymes are used repeatedly in production of ATP in the mitochondrion.

A

NAD/NADH, or nicotinamide adenine dinucleotide, and acetyl coenzyme A (ACA)
**crucial to maintaining life! do not degrade easily. will hang onto their vitamins

49
Q

phosphorylation of enzymes

A

will turn on the breakdown of glycogen

50
Q

zymogen or proenzyme

A

A pre-active enzyme

51
Q

what is the most important cellular antioxidant.

A

glutathione (GSH)

52
Q

For every molecule of oxidized glutathione (GSSG) two molecules of NADPH are required to reduce GSSG to GSH.

A

happy halloween!

53
Q

superoxide

A

(oxygen with an extra
electron: O2–1), leak from mitochondrial
respiration enzymes and wreak havoc on a cell.

54
Q

superoxidedismutase — SOD

A

an enzyme that detoxifies superoxide.

55
Q

enzyme catalase

A

detoxifies. the fastest enzyme yet discovered

56
Q

amyotrophic lateral sclerosis (ALS)

A

lou gerig’s disease. a degenerative disorder that leads to selective death of motor neurons in the brain and spinal chord, leading to gradually increasing paralysis over a few years.

57
Q

Cytochrome P450 Hemoprotein Enzymes

A

very nonspecific!–unusual as enzymes go, as they can catalyze a plethora of substrates
–They are found in all mitochondria, as
part of the electron transport chain of oxidative
phosphorylation. They can also be found in the lumen of endoplasmic reticulum in cells, performing many detoxification functions.

58
Q

Cytochrome P450 3A4

A

the most important cytochrome in cellular detoxification. This enzyme resides in the endoplasmic reticulum of cells.

59
Q

what does the liver do?

A

detoxifies or metabolizes drugs and toxic compounds, all foods, as well as metabolic products such as bilirubin (a breakdown product of
hemoglobin).

60
Q

cytochromes

A

the major enzymes involved in drug metabolism and drug bioactivation, accounting for ∼75% of total drug metabolism.

61
Q

induction

A

rapid metabolism

62
Q

inhibition

A

slow the breakdown of drugs

63
Q

hepatocytes

A

main cells in the liver

biochem_keubel (10 decks)

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