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Usually, they are named after the substrate whose decarboxylation they catalyze, for example pyruvate decarboxylase catalyzes the decarboxylation of pyruvate. Examples [ edit ]
Many of these vitamin K-dependent proteins are involved in coagulation so the function of the encoded enzyme is essential for hemostasis. [5] Most gla domain-containing proteins depend on this carboxylation reaction for posttranslational modification. [6] In humans, the gamma-glutamyl carboxylase enzyme is most highly expressed in the liver.
Control of Acetyl-CoA Carboxylase. The AMP regulated kinase triggers the phosphorylation of the enzyme (thus inactivating it) and the phosphatase enzyme removes the phosphate group. The regulation of mammalian ACC is complex, in order to control two distinct pools of malonyl-CoA that direct either the inhibition of beta oxidation or the ...
Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase [1] is a thiamine (vitamin B 1) derivative which is produced by the enzyme thiamine diphosphokinase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions.
Carboxylation is a chemical reaction in which a carboxylic acid is produced by treating a substrate with carbon dioxide. [1] The opposite reaction is decarboxylation.In chemistry, the term carbonation is sometimes used synonymously with carboxylation, especially when applied to the reaction of carbanionic reagents with CO 2.
Genetic disorders such as multiple carboxylase deficiency (MCD) (which includes biotinidase deficiency and holocarboxylase synthetase deficiency) [1] can also lead to inborn or late-onset forms of biotin deficiency. [2] In all cases – dietary, genetic, or otherwise – supplementation with biotin is the primary (and usually only) [3] method ...
Vitamin K is a family of structurally similar, fat-soluble vitamers found in foods and marketed as dietary supplements. [1] The human body requires vitamin K for post-synthesis modification of certain proteins that are required for blood coagulation ("K" from Danish koagulation, for "coagulation") or for controlling binding of calcium in bones and other tissues. [2]
It has been proposed that this thumb may function as a mobile lid for either, or possibly both, the biotin carboxylase or carboxyl- transferase active sites in the biotin-dependent enzyme (Cronan, 2001). The function of this lid could aid to prevent solvation of the active sites, thereby aiding in the transfer of CO 2 from carboxybiotin to ...