Canadian Medical Guide > Chemicals and Drugs > Enzymes and Coenzymes > Enzymes > Lyases > Carbon-Carbon Lyases Terms and Definitions

Carbon-Carbon Lyases

Medical Definition:	Enzymes that catalyze the cleavage of a carbon-carbon bond by means other than hydrolysis or oxidation. This subclass contains the DECARBOXYLASES, the ALDEHYDE-LYASES, and the OXO-ACID-LYASES. EC 4.1.
Guide Notes:	DF: C C LYASES
CAS Number:	EC 4.1

Carbon-Carbon Lyases Categories.

	Aldehyde-Lyases - Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.
	Carboxy-Lyases - Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
	Oxo-Acid-Lyases - Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
	Tryptophanase - An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. (From Enzyme Nomenclature, 1992) EC 4.1.99.1.
	Tyrosine Phenol-Lyase - An enzyme that catalyzes the cleavage of tyrosine to phenol, pyruvate, and ammonia. It is a pyridoxal phosphate protein. The enzyme also forms pyruvate from D-tyrosine, L-cysteine, S-methyl-L-cysteine, L-serine, and D-serine, although at a slower rate. EC 4.1.99.2.

Carbon-Carbon Lyases Medical Definitions and Terms

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