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Children with pyruvate carboxylase deficiency type A typically survive only into early childhood.
Carboxylation occurs in the liver and is performed by γ-glutamyl carboxylase.
An example of a moonlighting enzyme is pyruvate carboxylase.
Human acetyl-CoA carboxylase has recently become a target in the design of new anti-obesity drugs.
To some degree, it reverses the action of Acetyl-CoA carboxylase.
Pyruvate carboxylase deficiency is a rare condition, with an estimated incidence of 1 in 250,000 births worldwide.
The PC gene provides instructions for making an enzyme called pyruvate carboxylase.
It is formed by phosphoribosylaminoimidazole carboxylase.
In humans, the gamma-glutamyl carboxylase enzyme is most highly expressed in the liver.
Pyruvate carboxylase deficiency type B has life-threatening signs and symptoms that become apparent shortly after birth.
Pyruvate carboxylase deficiency is inherited as an autosomal recessive genetic condition.
In some cases, people with gene mutations that cause 3-methylcrotonyl-CoA carboxylase deficiency never experience any signs or symptoms of the disorder.
The carboxylase requires vitamin K as a cofactor and performs the reaction in a processive manner.
The enzyme that carries out the carboxylation of glutamic acid is gamma-glutamyl carboxylase.
It inhibits carboxylase, the enzyme that activates clotting factors and also shuts them down before they get out of hand.
Mutations in the PC gene cause pyruvate carboxylase deficiency.
Examples of enzymes activated in response to these changes are fructose 1,6-bisphosphatase, sedoheptulose bisphosphatase and ribulose-1,5-bisphosphate carboxylase.
The direct product of RuBP carboxylase reaction is glyceraldehyde-3-phosphate; these are subsequently used to make larger carbohydrates.
Researchers have identified at least three types of pyruvate carboxylase deficiency, which are distinguished by the severity of their signs and symptoms.
Phosphoenolpyruvic carboxylase may refer to:
Carboxylation by pyruvate carboxylase produces oxaloacetate.
A deficiency of pyruvate carboxylase can cause lactic acidosis as a result of lactate build up.
Individuals lacking functional biotinidase enzymes can still have normal carboxylase activity if they ingest adequate amounts of biotin.
By comparison, C4 carbon fixation via PEP carboxylase is more efficient.
Humans express the following two propionyl-CoA carboxylase isozymes: