Biochem Final (Esani)

Front 1

the ________(rxn) of amino acids produces __________(products)

Back 1

Deamination, ammonia

Front 2

define ureotelic

Back 2

(mammals) covert ammonia to urea for excretion

Front 3

define uricotelic

Back 3

(birds) convert ammonia to uric acid for excretion

Front 4

define ammonotelec

Back 4

(fish) secrete ammonia

Front 5

Amino acids are degraded into a _____ ______ and a ______ group (general)

Back 5

carbon sketeton and an amino group

Front 6

what are the 7 carbon skeletons that an amino acid can be degraded to?

Back 6

Acetyl CoA
Acetoacetyl CoA
Pyruvate
Alpha- ketoglutarate
Succinyl CoA
fumarate
Oxaloacetate

Front 7

define protein turnover

Back 7

the process of synthesis and degradation of proteins

Front 8

what is the protein turnover rate dependant on?

Back 8

dependant on the half lives of the proteins that are degraded

Front 9

what are the enzymes that degrade proteins

Back 9

calpain
lysosomal cathepsins
ubiquitin
proteosome

Front 10

what are the 3 mechanisms that promote protein degradation?

Back 10

N-terminal residues
proteins with PEST sequences
Oxidized residues of proteins

Front 11

which amino acid (N teminals residues) have long half lives? Short half lives?

Back 11

Long- methionine and alanine
Short- Leucine and lysine

Front 12

which proteins have PEST sequences?

Back 12

proline
glutamate
serine and threonine

Front 13

define Transamination

Back 13

transfer of alpha-amino group from one amino aid to and alpha-keto acid

Front 14

define Oxidative deamination

Back 14

ammonium formed when glutamate undergoes oxidative deamination

Front 15

are you capable of making a flow chart of sorts (or stating the system) for Urea synthesis?

Back 15

PROVE IT! (then look it up, its long and it wont fit here but good luck! I know you can answer correctly!)

Front 16

how is the urea cycle controlled?

Back 16

1) all five enzymes are altered by substrate availability
2) Glucogon
3) Carbamoyl phosphate synthetase I is activated by N-acetyl glutamate

Front 17

which amino acid (N teminals residues) have long half lives? Short half lives?

Back 17

Long- methionine and alanine
Short- Leucine and lysine

Front 18

which proteins have PEST sequences?

Back 18

proline
glutamate
serine and threonine

Front 19

define Transamination

Back 19

transfer of alpha-amino group from one amino aid to and alpha-keto acid

Front 20

define Oxidative deamination

Back 20

ammonio formed when glutamate undergoes oxidative deamination

Front 21

are you capable of making a flow chart of sorts (or stating the system) for Urea synthesis?

Back 21

PROVE IT! (then look it up, its long and it wont fit here but good luck! I know you can answer correctly!)

Front 22

how is the urea cycle controlled?

Back 22

1) all five enzymes are altered by substrate availability
2) Glucogon

Front 23

which amino acid (N teminals residues) have long half lives? Short half lives?

Back 23

Long- methionine and alanine
Short- Leucine and lysine

Front 24

which proteins have PEST sequences?

Back 24

P-proline
E-glutamate
S- serine
T-threonine

Front 25

define Transamination

Back 25

transfer of alpha-amino group from one amino aid to and alpha-keto acid

Front 26

define Oxidative deamination

Back 26

ammonio formed when glutamate undergoes oxidative deamination

Front 27

are you capable of making a flow chart of sorts (or stating the system) for Urea synthesis?

Back 27

PROVE IT! (then look it up, its long and it wont fit here but good luck! I know you can answer correctly!)

Front 28

how is the urea cycle controlled?

Back 28

1) all five enzymes are altered by substrate availability
2) Glucogon

Front 29

What classifies "hyperammonemia" result wise?

Back 29

NH+4>60 uL in the blood

Front 30

what are the symptoms for hyperammonemia?

Back 30

lethargy, tremors, slurred speech, blurred vision, protein-induced vomiting, coma and death

Front 31

what causes hyperammonemia?

Back 31

genetic and liver disease (cirrhosis)

Front 32

why is ammonia a neurotoxin in the brain?

Back 32

glutamate depletion, alpha-ketoglutarate depletion

Front 33

what is the fate of a carbon skeleton that form acetyl-CoA that are ketogenic?

Back 33

Phenylalanine,
Tyrosine
tryptophan
lysine
leucine

Front 34

fate of carbon skeletons that form pyruvate that are glucogenic

Back 34

ASCET
alanine
serine
cysteine
glycine
threonine

Front 35

def Alkaptonuria

Back 35

deficiency

Front 36

def albinism

Back 36

deficiency of tyrosinase

Front 37

def phenylketonuria

Back 37

deficiency of phenylalanine hydroxylase, build up of phenylalanine

Front 38

def MSD

Back 38

Maple Syrup Disease (branched chain ketoaciduria) deficiency of alpha ketoacid dehydrogenase complex

Front 39

def methyl malonic acidemia

Back 39

deficiency of methylmalonyl CoA mutase

Front 40

def alkaptonuria and what happens

Back 40

deficiency of homogentisate oxidase, urine turns black on exposure to air (oxidized)

Front 41

def Albinism and what happens

Back 41

deficiency of tyrosinase, a lack of product melanin, albinos lack pigament, susceptible to skin cancer and sunburn

Front 42

def phenylketonuria, and what happens

Back 42

deficiency of phenylalanine hydroxylase, lack of enzyme leads to mental retardation in infants, damage due to accumulated phenylalanine

Front 43

What is the pathogenisis of MSD

Back 43

accumulate alpha ketoacids from Leu and Iso and Val, gives urine odor of maple syrup

Front 44

Pathogenisis of MMA

Back 44

methyl malonic acidemia- deficiency of methylmalonyl (CoA mutase),
accumulates due to deficiency of adenosyl cobalamin or weak binding of CoA enzyme by defective enzyme. B12 treatment

Front 45

what degrades acetylcholine

Back 45

acetylcholinesterase

Front 46

what oxidizes and methylates catecholamines and what are the products?

Back 46

O: monoamine oxidase
M: catechol-O-methyltransferase
P: metanephrine, VMA (vanillylmandelic acid)

Front 47

what enzymes degrade dietary and local nucleotides?

Back 47

DNases
RNases
Phosphodiesterases
Nucleosidases

Front 48

what do purines degrade to?

Back 48

uric acid

Front 49

excess uric acid causes what (clinically)?

Back 49

Gout

Front 50

How is gout caused?

Back 50

uric acid deposits in the kidnes and joints which is caused by increaced synthesis of purine or under-secretion of uric acid

Front 51

can you degrade the rings of: Purine? Pyrimidine?
if they can, what does it degrade to?

Back 51

NO!
YES!
the pyrimidine rings degrades to beta-alanine and beta-aminoisobutyrate (then to acetyl CoA and succinyl CoA

Front 52

Heme degrades to ______, in the (3 locales in the body).

Back 52

bilirubin
1) reticuloendothelial cells of the liver
2) spleen
3) bone marrow

Front 53

What happens to excess amino acids?

Back 53

they are degraded (not branched chained-L, I, V)

Front 54

Which demographic of persons need a positive nitrogen balance?

Back 54

Pregnant women

Front 55

What is the name for the syndrome when one has a negative nitrogen balance? What happens?

Back 55

Kwashiorkor- mother gets a disease from having a negative nitrogen balance (has had one child and second on the way, both children are depleting her of nitrogen)

Front 56

What Amino Acids MUST be consumed?

Back 56

ILL, 3-9, trip val
Isoleucine, Leucine, Lysine
Methionine, Phenylalanine, Threonine
Tryptophan, Valine

Front 57

first step of amino acid synthesis is to:

Back 57

transport formed or essential amino acids across the plasma membranes

Front 58

what is required for Transanination to occure?

Back 58

aminotransferase and pyridocal-5-phosphate (B6 derive)

Front 59

most commonly used amino acid group donor during transamination is:

Back 59

Glutamate

Front 60

what is the transamination pair for: alpha ketoglutarate

Back 60

glutamate

Front 61

what is the transamination pair for:oxaloacetate

Back 61

aspartate

Front 62

what is the transamination pair for: Pyruvate

Back 62

alanine

Front 63

using direct amination, create glutamate

Back 63

NH4+ and an Alpha-ketoglutarate= glutamate
(NADPH+H=NADP+ and NADH+H=NAD+)

Front 64

using glutamine synthase, create glutamine

Back 64

glutamate+ATP+NH4(+)= Glutamine +ADP+Pi

Front 65

what happens in reductive amination?

Back 65

amino groups are transferred from one carbon atom to another

Front 66

what are the products from the precursor: glycerate-3-phosphate

Back 66

serine, glycine, cysteine

Front 67

what are all the products from the precursor: oxaloacetate

Back 67

aspartate, asparagine, lysine, methionine, threonine

Front 68

what are the products from the precursor: pyruvate

Back 68

AVALI
amino acids, alanine, valine, leucine, isoleucine

Front 69

what are the product from the precursor: phenylalanine

Back 69

tyrosine

Front 70

what are the product from the precursor: phospho-ribosyl-pyrophosphate

Back 70

histidine

Front 71

what carries many of the oxidation forms of one-carbon molecules?

Back 71

folic acids reduced form: tetrahydrofolic acid

Front 72

Pernicious anemia

Back 72

Vit B12 deficiency where Intrensic factor is not produced in the stomach, leading to no absorbtion of B12.

Front 73

What is SAM and what does it do?

Back 73

S-adenosylmethionine, it is a carrier of methyl groups

Front 74

what are some methylation products?

Back 74

phosphotidalcholine, epinephrine, creatine, carnithine

Front 75

what is glutathione used for?

Back 75

synthesis,
reducing agent (protect from ROS)
transport

Front 76

what complex is used to transport amino acids, cysteine and methionine through the cell membrane via the gamma glutamyl cycle?

Back 76

glutathione

Front 77

what are 2 excitatory neurotransmitters?

Back 77

glutamate and acetylcholine

Front 78

what does an inhibitory neurotransmitter do?

Back 78

opens chloride channels in the membrane and inhibits the formation of the action potential

Front 79

wha is an example of an inhibitory neurotransmitter?

Back 79

Glycine

Front 80

what is GABA? how is it made? what does it do?

Back 80

Gamma AminoButyric Acid, produced by decarboxylating glutamate. GABA binds to a nerve cell and increases permeability to CL

Front 81

if a patient suffered from anxiety or aggressive behavior, what would yo give them?

Back 81

Benzodiazepine tranq's- enhances GABA ability to bind

Front 82

what are 3 catecholamines?

Back 82

norepinephrine
epinepherine
dopamine

Front 83

how is parkinsons disease caused?

Back 83

a deficiency of dopamine which results in a neurological degeneration

Front 84

which catecholamines are excitatory neurotransmitters?

Back 84

norepinephrine and dopamine

Front 85

which catecholamines are hormones of carb and lipid metabolism?

Back 85

norepinephrine and epinephrine

Front 86

catecholamines are derivatives of what? where are they produced?

Back 86

tyrosine, produced in the CNS and adrenal medulla

Front 87

(general) what is a nucleotide made from?

Back 87

a nitrogenous base, ribose sugar, and a phosphate group

Front 88

def tautomeric

Back 88

purines and pyrimidines are tautomeric- means they shift double bonds and hydrogen position

Front 89

what is the Salvage Pathway?

Back 89

purines are produced from PRPP and hypoxanthine or guanine, energy saving

Front 90

what is the regulation of purine synthesis?

Back 90

PRPP substrate availability,
[AMP] and [GTP] regul. metabolism of IMP
AMP and GTP regulates the others production

Front 91

what are the three pyrimidines?

Back 91

thyamine, cytosine, and uracil

energy using production

Front 92

how is heme produced?

Back 92

porphyrin ring is produced from condensation of glycine and syccinyl CoA