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ετυμολογία

Τι (ποιος) είναι pyruvate carboxylase - ορισμός

MAMMALIAN PROTEIN FOUND IN HOMO SAPIENS

Pyruvate carboxyltransferase; Pyruvate carboxytransferase; EC 6.4.1.1; Pyruvate:carbon-dioxide ligase (ADP-forming)

Pyruvate dehydrogenase deficiency

CARBOHYDRATE METABOLIC DISORDER CHARACTERIZED BY THE BUILDUP OF LACTIC ACID IN THE BODY AND A VARIETY OF NEUROLOGICAL PROBLEMS AND CAUSED BY A DEFICIENCY OF ONE OF THE THREE ENZYMES IN THE PYRUVATE DEHYDROGENASE COMPLEX

Pyruvate dehydrogenase complex deficiency disease; Deficiency of pyruvate dehydrogenase

Pyruvate dehydrogenase deficiency (also known as pyruvate dehydrogenase complex deficiency or PDCD) is a rare neurodegenerative disorders associated with abnormal mitochondrial metabolism. PDCD is a genetic disease resulting from mutations in one of the components of the pyruvate dehydrogenase complex (PDC).

https://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_deficiency

Methylcrotonyl-CoA carboxylase

CLASS OF ENZYMES

Methylcrotonoyl-CoA carboxylase; MCCC2; MCCC1; 3-methylcrotonyl-CoA carboxylase; EC 6.4.1.4; 3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming); MC-CoA carboxylase

Methylcrotonyl CoA carboxylase (, MCC) (3-methylcrotonyl CoA carboxylase, methylcrotonoyl-CoA carboxylase) is a biotin-requiring enzyme located in the mitochondria. MCC uses bicarbonate as a carboxyl group source to catalyze the carboxylation of a carbon adjacent to a carbonyl group performing the fourth step in processing leucine, an essential amino acid.

https://en.wikipedia.org/wiki/Methylcrotonyl-CoA_carboxylase

Lysine—pyruvate 6-transaminase

CLASS OF ENZYMES

Lysine--pyruvate 6-transaminase; Lysine-pyruvate 6-transaminase; EC 2.6.1.71; L-lysine:pyruvate aminotransferase

In enzymology, a lysine-pyruvate 6-transaminase () is an enzyme that catalyzes the chemical reaction

https://en.wikipedia.org/wiki/Lysine—pyruvate_6-transaminase

Βικιπαίδεια

Pyruvate carboxylase

Pyruvate carboxylase (PC) encoded by the gene PC is an enzyme (EC 6.4.1.1) of the ligase class that catalyzes (depending on the species) the physiologically irreversible carboxylation of pyruvate to form oxaloacetate (OAA).

The reaction it catalyzes is:

pyruvate + HCO⁻
₃ + ATP → oxaloacetate + ADP + P

It is an important anaplerotic reaction that creates oxaloacetate from pyruvate. The enzyme is a mitochondrial protein containing a biotin prosthetic group, requiring magnesium or manganese and acetyl-CoA.

Pyruvate carboxylase was first discovered in 1959 at Case Western Reserve University by M. F. Utter and D. B. Keech. Since then it has been found in a wide variety of prokaryotes and eukaryotes including fungi, bacteria, plants, and animals. In mammals, PC plays a crucial role in gluconeogenesis and lipogenesis, in the biosynthesis of neurotransmitters, and in glucose-induced insulin secretion by pancreatic islets. Oxaloacetate produced by PC is an important intermediate, which is used in these biosynthetic pathways. In mammals, PC is expressed in a tissue-specific manner, with its activity found to be highest in the liver and kidney (gluconeogenic tissues), in adipose tissue and lactating mammary gland (lipogenic tissues), and in pancreatic islets. Activity is moderate in brain, heart and adrenal gland, and least in white blood cells and skin fibroblasts.

https://en.wikipedia.org/wiki/Pyruvate carboxylase