Biochem (Enzymzes mostly) Flashcards

1
Q

Phosphorylase, Amylo-1,6 glucosidase debranching enzyme

A

Mobilization of glucose from glycogen: glycogenolysis

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2
Q

Galactokinase; Galactose-1-P uridylytransferase

A

Galactose to Galactose-1-P, inhibition leads to non-classical galactosemia; galactose1P to UDPgalactose to UDPglucose to Glucose1P, inhibition leads to classical galactosemia

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3
Q

Regulators of Glucokinase;PFK1;Pyruvate kinase

A

Glucose, regulatory subunit; Citrate, ATP -, AMP, Fructose 2,6 Biphosphate +; Fructose 1,6 Biphosphate+, ATP-

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4
Q

activation and transport of fatty acids

A

Palmitoyl CoA ligase, Caritine acyltransferase I,II, Carnitine acylcarnitine translocase

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5
Q

Odd chain fatty acid oxidation

A

Vitamin B12, Propionyl-CoA carboxylase, Biotin, CO2

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6
Q

Regulation of pyruvate dehydrogenase

A

ADP, pyruvate - to inhibitory kinase; NADH, Acetyl CoA inhibitory to activating phosphatase, Intracellular calcium stimluates phosphatase
3 units, located in the mt matrix

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7
Q

NADH producting steps in TCA

A

isocitrate dehydrogenase, alpha ketoglutarte, succinate dehydrogenae (FAD), malate dehydrogenase

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8
Q

Reguation of TCA enzmyes

A

ADP, Ca + for a ketoglutarate and isocitrate dehydrogenase, NADH - for all dehydrogenases

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9
Q

Glucose 6 phosphate dehydrogenase

A

Pentose phosphate pathway, NADPH production

Makes nucleotides or fructose-6-phosphate or glyceraldehyde-3-phosphate

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10
Q

Pyruvate Carboxylase

A

Pyruvate to OAA, Acetyl CoA +

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11
Q

Acetyl CoA carboxylase

A

acetyl co A to malonyl coA, citrate/insulin+, palmitoyl CoA-

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12
Q

Glycogen synthase, branching enzyme

A

Glycogen synthesis

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13
Q

Carbamoyl Phosphate Synthetase I

A

Conversion to carbamoyl phosphate, allosterically upregulated by N-acetyl glutamate whose production is upregulated by arginine

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14
Q

arginosuccinate

A

catalyzes the conversion of arginosuccinate to arginine; byproduct is fumarate

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15
Q

AA’s that form OAA

A

Asp, Asn

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16
Q

AA’s that form aKG

A

Glutamate, glutamine, proline, histidine, arginine

17
Q

AA’s that form pyruvate

A

alanine, serine, glycine, cysteine, threonine

18
Q

AA’s that form fumarate

A

phenylalanine, tyrosine

19
Q

AA’s that form succinyl coA

A

methionine, valine, isoleucine, threonine

20
Q

Nonessential amino acids

A

Asp, Asn, Glu, Gln, Ala, Ser, Gly, Cys, Arg, Pro, Tyr

21
Q

ribonucleotide reductase

A

ribonucleoside diphosphate to deoxyribonucleoside diphosphate

22
Q

OXPHOS (membrane transporters and their location)

A

Adenine nucleotide translocase, Phosphate/pyruvate symporter, Calcium uniporter

23
Q

Competitive inhibition

A

Bind at substrate recognition site prevent substrate from binding, increasing substrate concentration can overcome competitive inhibitors, increase Km and no effect on Vmax

24
Q

Noncompetitive inhibitors

A

Interfere with binding site not with primary substrate, lower Vmax

25
Q

Uncompetitive inhibition

A

Bind only to enzyme containing substrate, decrease Vmax and Km

26
Q

Mechanism based inhibitors

A
  1. Reactive inhibitors are substrate analogs with highly reactive functional groups
  2. Transition state analogs
  3. Heavy metals that react with amino acid side chains
27
Q

Active site in enzymes

A

A. Substrates interact with active sites by multiple weak interactions
B. large changes in protein confirmation upon substrate binding
C. Side chain stabilization, coenzymes, metal ions

28
Q

Fructose entrance into glycolysis

A

Fructose–>fructose-1-P–>DHAP+glyceraldehyde–>glyceraldehyde -3-P

29
Q

Michaelis-Menten equation

A

vi=Vmax[S]/(Km+[S]

30
Q

Lineweaver-Burk Transformation

A

x intercept is negative inverse Km while y intercept is inverse Vmax

31
Q

Coenzmyes of TCA

A

NAD/FAD/CoASh

32
Q

Glutamate Dehydrogenase

A

Ammonia + alpha keto glutarate –> Glutamate
Forward reaction- reductive amination, GTP down-regulated
Reverse reaction- oxidative deamination, ADP up-regulated