This quiz from Chapter 18 focuses on amino acid oxidation and urea production, assessing knowledge on proteases in the small intestine, zymogens, and critical enzymes like enteropeptidase and transaminases. It's essential for students understanding biochemical pathways and enzyme functions.
Biotin phosphate.
Lipoic acid.
Nicotinamide adenine dinucleotide phosphate (NADP+).
Pyridoxal phosphate (PLP).
Thiamine pyrophosphate (TPP).
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Brain.
Kidney.
Liver.
Skeletal muscle.
Small intestine.
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Niacin.
Pyridoxine (vitamin B6).
Riboflavin.
Thiamin.
Vitamin B12.
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Aspartate.
Carnitine.
Pyruvate.
Tyrosine.
Urea.
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Biotin.
NADH.
No coenzyme is involved.
Pyridoxal phosphate (PLP).
Thiamine pyrophosphate (TPP).
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High carbohydrate, very low protein
Very high carbohydrate, no protein, no fat
Very very high fat, high carbohydrate, no protein
Very high fat, very low protein
Very low carbohydrate, very high protein
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Aspartate
ATP
Carbamoyl phosphate
Malate
Ornithine
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Decarboxylation requiring thiamine pyrophosphate (TPP).
Hydroxylation requiring NADPH and O2.
Oxidative deamination requiring NAD+.
Reduction requiring pyridoxal phosphate (PLP).
Transamination requiring pyridoxal phosphate (PLP).
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Does not require any cofactors.
Is a reductive deamination.
Is accompanied by ATP hydrolysis catalyzed by the same enzyme.
Is catalyzed by glutamate dehydrogenase.
Requires ATP.
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Fumarate.
Pyruvate.
Succinate.
Alpha-ketoglutarate.
None of the above.
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Cleavage of urea to ammonia.
Formation of citrulline from ornithine and another reactant.
Formation of ornithine from citrulline and another reactant.
Formation of urea from arginine.
Transamination of arginine.
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Glutamic acid
Serine
Threonine
Tyrosine
Proline
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1 and 5
1, 3, and 5
2 and 4
2, 3, and 4
2, 4, and 5
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Deficiency of protein in the diet.
Inability to catabolize ketone bodies.
Inability to convert phenylalanine to tyrosine.
Inability to synthesize phenylalanine.
Production of enzymes containing no phenylalanine.
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Adenine
Aspartate
Creatinine
Glutamate
Ornithine
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Oxaloacetate.
Propionate.
Pyruvate.
Succinate.
Succinyl-CoA
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Deamination.
Hydrolysis.
Oxidative deamination.
Reductive deamination.
Transamination.
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Krebs was a major contributor to the elucidation of the pathway involved.
The amino acid arginine is the immediate precursor to urea.
The carbon atom of urea is derived from mitochondrial HCO3–.
The precursor to one of the nitrogens of urea is aspartate.
The process of urea production is an energy-yielding series of reactions.
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Alanine
Aspartic acid
Asparagine
Serine
Threonine
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1 and 4
1, 2 and 4
1, 3 and 5
2, 4 and 5
4 and 5
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It is similar to transamination in that it involves the coenzyme pyridoxal phosphate (PLP).
NH4+ is produced.
The enzyme can use either NAD+ or NADP+ as a cofactor.
The enzyme is glutamate-specific, but the reaction is involved in oxidizing other amino acids.
Alpha-Ketoglutarate is produced from an amino acid.
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Chymotrypsin
Elastase
Enteropeptidase
Secretin
Trypsin
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Enteropeptidase
Hexokinase
Papain
Pepsin
Secretin
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Electrons
H+
Acyl groups
One carbon units
NH2 groups
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Chymotrypsinogen
Pepsin
Pepsinogen
Trypsin
Trypsinogen
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A deficiency of the vitamin niacin.
Oxidative decarboxylation.
Synthesis of branched chain amino acids.
Transamination of an amino acid.
Uptake of branched chain amino acids into liver.
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