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
Uncompetitive inhibition
Bind only to enzyme containing substrate, decrease Vmax and Km
26
Mechanism based inhibitors
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
Active site in enzymes
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
Fructose entrance into glycolysis
Fructose-->fructose-1-P-->DHAP+glyceraldehyde-->glyceraldehyde -3-P
29
Michaelis-Menten equation
vi=Vmax[S]/(Km+[S]
30
Lineweaver-Burk Transformation
x intercept is negative inverse Km while y intercept is inverse Vmax
31
Coenzmyes of TCA
NAD/FAD/CoASh
32
Glutamate Dehydrogenase
Ammonia + alpha keto glutarate --> Glutamate Forward reaction- reductive amination, GTP down-regulated Reverse reaction- oxidative deamination, ADP up-regulated