Amino Acid metabolism

Question 1

origin of all reduced nitrogen compounds in our metabolism

Answer 1

nitrogen fixation

Question 2

steps required for amino acid degradation

Answer 2

transaminase and glutamate dehydrogenase

Question 3

do all amino acids have their own enzyme that does the transamination reaction

Answer 3

yes

Question 4

central molecules for transamination reactions

Answer 4

glutamate and a-ketoglutarate

Question 5

is transamination reversible

Answer 5

yes

Question 6

where is glutamate dehydrogenase

Answer 6

inner mitochondrial membrane

Question 7

what does glutamate dehydrogenase regenerate

Answer 7

a-kg

Question 8

is glutamate dehydrogenase reversible

Answer 8

yes

Question 9

what converts glutamine to glutamate

Answer 9

glutamine synthetase

Question 10

what does going from glutamate to glutamine require

Answer 10

ATP

Question 11

synthase

Answer 11

no energy from NTP

Question 12

synthetase

Answer 12

involvement of NTP

Question 13

cofactor for transamination

Answer 13

PLP

Question 14

mechanism for PLP

Answer 14

schiff base

Question 15

gluconeogenic amino acids enter as

Answer 15

pyruvate or tca intermediates

Question 16

ketogenic amino acids enter as

Answer 16

acetyl coa

Question 17

deamining alanine leads to

Answer 17

pyruvate

Question 18

deaminiating serine leads to

Answer 18

pyruvate

Question 19

after removing the nitrogen of a BCAA, what is the pathway similar to

Answer 19

tca cycle and b-oxidation

Question 20

why does pku lead to neurological defects

Answer 20

tyrosine is used for dopamine, without it cant do it

Question 21

maple syrup urine disease

Answer 21

branched-chain alpha keto acid dehydrogenase deficiency

Question 22

urea characteristics

Answer 22

highly oxidized (no leftover energy in C)
high ratio of N to C
very soluble in H2O

Question 23

the urea cycle removes _____ and returns ______

Answer 23

urea, ornithine

Question 24

the urea cycle ties into

Answer 24

transamination, citric acid cyle, and carbamoyl phosphate

Question 25

vitamins

Answer 25

more stable versions of coenzymes that are slightly modified in our bodies to reactive forms that are used by enzymes

Question 26

tetrahydrogolate used to move

Answer 26

methyl methylene formyl

Question 27

cobalamins is

Answer 27

vit b12

Question 28

special property of cobalamins

Answer 28

carbon-cobalt bond is weak

Question 29

cobalamin carries

Answer 29

methyl group

Question 30

special chemistry in cobalamin

Answer 30

radical chemistyr

Question 31

SAM moves a

Answer 31

methyl group

Question 32

used up version of SAM

Answer 32

s-adenosylhomocysteine

Question 33

s-adenosylmethionine used for

Answer 33

methylating DNA (epigenetics)

Question 34

asparagine synthetase reaction

Answer 34

aspartate -> asparagine

Question 35

glutamate synthetase reaction

Answer 35

glutamate -> glutamine

Question 36

where do animals synthesize cysteine from

Answer 36

methionine

Question 37

where do plants and bacteria synthesize cysteine from

Answer 37

inorganic sulfur and synthesize methionine from cysteine

Question 38

one of the most metabolically active amino acids

Answer 38

glutamate

Question 39

cofactor for collagen synthesis

Answer 39

vit C

Question 40

what does shikimate pathway

Answer 40

phenylalanine, tyrosine, tryptophan

Question 41

roundup inhibits the

Answer 41

shikimate pathway

Question 42

biosynthesis of histidine starts with

Answer 42

nucleotide

Question 43

why cant we synthesize essential amino acids

Answer 43

no enzyme to synthesize historically have had amino acids available, no need to make

Question 44

glycine and proline important in

Answer 44

collagen

Question 45

nonessential amino acids

Answer 45

need a lot of them so synthesize

Question 46

aspartate can make

Answer 46

methionine threonine lysine

Question 47

glutamate can make

Answer 47

glutamine proline arginine

Question 48

nitrogen metabolism steps

Answer 48

assimilation (from ammonia) redistriution (transaminatio) disposal (urea cycle)

Question 49

are transaminases used in both amino ______ and _____ pathways

Answer 49

biosynthesis and degradation

Question 50

point of glutamate dehydrogenase

Answer 50

regenerates alpha-ketoglutarate for transaminations

Question 51

product of glutamate dehyudrogenase rxn taken where

Answer 51

NH3, urea cycle

Question 52

branched chain amino acids, after removing ____, similar steps to what and waht produced

Answer 52

N, citric acid cyle, carbohydrates and/or acetyl coa

Question 53

steps of BCAA degradation

Answer 53

1st remove N transamination oxidative decarboxylation acyl-coa dehydrogenation hydration dehydrogenation thiolytic cleavaege

Question 54

folate is a ____ and contains ______

Answer 54

coenzyme, glutamate

Question 55

THF used in

Answer 55

AA degradation and synthesis

Question 56

major roles of folate, adenosylcobalamin, SAM

Answer 56

aceept or donate 1C

Question 57

what kind of reactions do folate, adenosylcobalamin, and SAM

Answer 57

single methyl transfers ex: generating valine

Question 58

pyruvate -> oxaloacetate -> a-ketoglutarate ->

Answer 58

alanine aspartate glutamate

Question 59

asparagine synthetase

Answer 59

aspartate -> asparagine

Question 60

glutamine synthetase

Answer 60

glutamate -> glutamine

Question 61

what does vit c pull into collagen formation

Answer 61

a-kg to succinate