The sucrose substitute tagatose is produced by hydrolyzing lactose and then chemically converting one of the two resulting aldoses to a ketose. Which residue of lactose gives rise to tagatose?
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The sucrose substitute tagatose is produced by hydrolyzing lactose and then chemically converting one of the two resulting aldoses to a ketose. Which residue of lactose gives rise to tagatose?
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- Phosphopentose isomerase interconverts the aldose ribose 5-phosphate and the ketose ribulose 5-phosphate. Propose a mechanism.Explain the chemical change that occurs in converting kynurenine (a product of tryptophan degradation) to kynurenate, a reaction in which α-ketoglutarate is transformed to glutamate.What is the physiological significance of the isozymic forms of lactate dehydrogenase (LDH)? Explain briefly.
- An oligosaccharide is a repeating unit of a-D-galactopyranosyl-(a-1 >3)-allopyranoside. Each disaccharide unit is linked via B-1 --->4 glycosidic bond. The oligosaccharide has 10 monosaccharide residues. Required: Is this oligosaccharide a good substrate for glycolysis? Why or why not? Provide two reasons and discuss corn prehensively.Palmitic acid is a straight-chain saturated 16-carbon fatty acid. How many moles of malonyl-CoA are required for the synthesis of one mole of palmitic acid?An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?
- The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?How is synthesis and degradation of fructose-2,6-bisphosphate achieved?Which of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.