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Introduction Vitamin K is an essential fat-soluble micronutrient, which is required for a novel post-translational chemical modification in a miniscule group of proteins with calcium-binding properties, known generally as vitamin K-dependent proteins or Gla proteins. This far, the only unquestioned role of vitamin K in health is in the upkeep of normal coagulation. The vitamin K dependent coagulation proteins are synthesized in the liver and comprise factors II, VII, IX, and X, which have a haemostatic role ( i.e. They are procoagulants that arrest and forestall bleeding ), and proteins C and S, which have an anticoagulant role ( i.e. They hold back the clotting process ). Despite this duality of function, the overriding effect of nutritive vitamin K deficiency is a bleeding disposition because of the relative immobility of the procoagulant proteins.
Vitamin K-dependent proteins synthesized by other tissues include the bone protein osteocalcin and matrix Gla protein, though their functions wait to be explained. Biological role of vitamin K is the family name for a collection of fat-soluble compounds which have a standard 2-methyl-1,4-naphthoquinone nucleus but differ in the structures of a side chain at the 3-position.
Vitamin K are synthesized by plants and bacteria. In plants the only significant molecular form is phylloquinone ( vitamin K1 ) that has a phytyl side chain.
Bacteria synthesize a family of compounds called menaquinones ( vitamin K2 ), which have side chains based fully on repeating unsaturated 5-carbon ( prenyl ) units. These are delegated menaquinone-n ( MK-n ) according to the number ( n ) of prenyl units. Some bacteria also synthesize menaquinones in which a few of the double bonds is saturated. The compound 2-methyl-1,4-naphthoquinone ( common name menadione ) could be accepted as a provitamin because vertebrates can change it to MK-4 by adding a 4-prenyl side chain at the 3-position.
The biological role of vitamin K is to act as a cofactor for a specific carboxylation reaction that transforms selective glutamate. .
Introduction Vitamin K is an essential fat-soluble micronutrient, which is required for a novel post-translational chemical modification in a miniscule group of proteins with calcium-binding properties, known generally as vitamin K-dependent proteins or Gla proteins. This far, the only unquestioned role of vitamin K in health is in the upkeep of normal coagulation. The vitamin K dependent coagulation proteins are synthesized in the liver and comprise factors II, VII, IX, and X, which have a haemostatic role ( i.e. They are procoagulants that arrest and forestall bleeding ), and proteins C and S, which have an anticoagulant role ( i.e. They hold back the clotting process ). Despite this duality of function, the overriding effect of nutritive vitamin K deficiency is a bleeding disposition because of the relative immobility of the procoagulant proteins.
Vitamin K-dependent proteins synthesized by other tissues include the bone protein osteocalcin and matrix Gla protein, though their functions wait to be explained. Biological role of vitamin K is the family name for a collection of fat-soluble compounds which have a standard 2-methyl-1,4-naphthoquinone nucleus but differ in the structures of a side chain at the 3-position.
Vitamin K are synthesized by plants and bacteria. In plants the only significant molecular form is phylloquinone ( vitamin K1 ) that has a phytyl side chain.
Bacteria synthesize a family of compounds called menaquinones ( vitamin K2 ), which have side chains based fully on repeating unsaturated 5-carbon ( prenyl ) units. These are delegated menaquinone-n ( MK-n ) according to the number ( n ) of prenyl units. Some bacteria also synthesize menaquinones in which a few of the double bonds is saturated. The compound 2-methyl-1,4-naphthoquinone ( common name menadione ) could be accepted as a provitamin because vertebrates can change it to MK-4 by adding a 4-prenyl side chain at the 3-position.
The biological role of vitamin K is to act as a cofactor for a specific carboxylation reaction that transforms selective glutamate. .
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