Vitamins requirements

Vitamin A [79-80-1] (6) is stmcturaHy similar to vitamin A [68-26-8] and is also found in fish oils. This compound is important biologically for fish and other lower animals. Interestingly, tadpoles require vitamin A but after metamorphosis require vitamin A (8). 

C. You will require vitamin B12 injections monthly for life. 

Peptidyl hydroxyprohne and hydroxylysine are formed by hydroxylation of peptidyl proline or lysine in reactions catalyzed by mixed-function oxidases that require vitamin C as cofactor. The nutritional disease scurvy reflects impaired hydroxylation due to a deficiency of vitamin C. 

For activity, factors II, VII, IX, and X and proteins C and S require vitamin K-dependent y-carboxylation of certain glutamate residues, a process that is inhibited by the anticoagulant warfarin. 

The solution to the assay problem came from the fortunate finding by Mary Schorb, then working in the poultry industry, of a microorganism, Lactobacillus lactis dorner, which required vitamin B]2 for growth. With much quicker and more reliable assays the vitamin was isolated in 1948 in both the Merck and Glaxo laboratories. Its structure was determined by X-ray crystallography by Lenhert and Hodgkin (1961). 

As indicated in Section 6.3.3 and Table 6.2 the key control step is mediated by glycogen phosphorylase, a homodimeric enzyme which requires vitamin B6 (pyridoxal phosphate) for maximum activity, and like glycogen synthase (Section 6.2) is subject to both allosteric modulation and covalent modification. 

In addition to methanogens and some acetogens, bacteria capable of 1,2-propanediol fermentation have been reported to produce vitamin B12 [286]. The transformation of 1,2-propanediol (propylene glycol) to propionaldehyde requires vitamin B12. Further fermentation of propionaldehyde to n-propanol and propionic acid does not require vitamin B12 but yields energy for growth. 

Answer E. The patient has many signs of scurvy from a vitamin C deficiency. The diet, which contains no fruits or vegetables, provides little vitamin C, Prolyl hydroxylase requires vitamin C, and in the absence of hydroxylation, the collagen a-chains do not form stable, mature collagen. The anemia may be due to poor iron absorption in the absence of ascorbate. 

Additional folate may be stored as the highly reduced JV -methyl-THF. This form is referred to as the storage pool as there is only one known enzyme that uses it, and in turn moves it back into the active pool. This enzyme is N-methyl THF-homocysteine methyltransferase, discussed above, which also requires vitamin and is involved in regenerating SAM as a methyl donor for reactions. 

Answer D. Sideroblastic anemia in a person being treated for tuberculosis (with isoni-azid) is most likely due to vitamin deficiency. 6-Aminolevulinate synthase, the first enzyme in heme synthesis requires vitamin Bj (pyridoxine). 

Figure 22.7 Homocysteine formation from methionine and formation of thiolactone from homocysteine. The homocysteine concentration depends upon a balance between the activities of homocysteine methyltransferase (methionine synthase) and cystathionine p-synthase. Both these enzymes require vitamin B12, so a deficiency can lead to an increase in the plasma level of homocysteine. (For details of these reactions, see Chapter 15.) Homocysteine oxidises spontaneously to form thiolactone, which can damage cell membrane.

Vitamin C is L-ascorbic acid (chemically 2-oxogulonolactone). The two hydroxyl groups have acidic properties. By releasing a proton, ascorbic acid therefore turns into its anion, ascorbate. Humans, apes, and guinea pigs require vitamin C because they lack the enzyme L-gulonolactone oxidase (tl.3.8), which catalyzes the final step in the conversion of glucose into ascorbate. 

Two essential enzymatic reactions in humans require vitamin B12 (Figure 33-2). In one, methylcobalamin serves as an intermediate in the transfer of a methyl group from /V5-methyltetrahydrofolate to homocysteine, forming methionine (Figure 33-2A Figure 33-3, section 1). Without vitamin B12, conversion of the major dietary and storage folate, N5-... 

The other reaction that requires vitamin B12 is isomerization of methylmalonyl-CoA to succinyl-CoA by the enzyme methylmalonyl-CoA mutase (Figure 33-2B). In vitamin B12 deficiency, this conversion cannot take place and the... 

Extra carboxyl groups may be added to Glu residues of some proteins. For example, the blood-clotting protein prothrombin contains a number of y-carboxygluta-mate residues (Fig. 27-29b) in its amino-terminal region, introduced by an enzyme that requires vitamin K. These carboxyl groups bind Ca2+, which is required to initiate the clotting mechanism. 

There are two major disposal pathways for homocysteine. Conversion to methionine requires folate and vitamin B12-derived cofactors. The formation of cysteine requires vitamin B6(pyridoxine). 

Oxidation of fatty acids with an odd number of carbons proceeds two carbons at a time (pro ducing acetyl CoA) until the last three carbons (propionyl CoA). This compound is con verted to methylmalonyl CoA (a reaction requiring biotin), which is then converted to succinyl CoA by methylmalonyl CoA mutase (requiring vitamin B )- A genetic error in the mutase or vitamin B12 deficiency causes methylmalonic acidemia and aciduria. 

The human body contains only about 1.5 mg of cobalt, almost all of it is in the form of cobalamin, vitamin B12. Ruminant animals, such as cattle and sheep, have a relatively high nutritional need for cobalt and in regions with a low soil cobalt content, such as Australia, cobalt deficiency in these animals is a serious problem. This need for cobalt largely reflects the high requirement of the microorganisms of the rumen (paunch) for vitamin B12. All bacteria require vitamin B12 but not all are able to synthesize it. For example, E. coli lacks one enzyme in the biosynthetic... 

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