|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
In enzymology, a carboxylesterase (EC 184.108.40.206, ali-esterase, B-esterase, monobutyrase, cocaine esterase, procaine esterase, methylbutyrase, vitamin A esterase, butyryl esterase, carboxyesterase, carboxylate esterase, carboxylic esterase, methylbutyrate esterase, triacetin esterase, carboxyl ester hydrolase, butyrate esterase, methylbutyrase, alpha-carboxylesterase, propionyl esterase, nonspecific carboxylesterase, esterase D, esterase B, esterase A, serine esterase, carboxylic acid esterase, cocaine esterase) is an enzyme that catalyzes the chemical reaction
- a carboxylic ester + H2O an alcohol + a carboxylate
Most enzymes from this group belong to the superfamily of hydrolases with alpha/beta protein fold (so called Alpha/beta hydrolase fold), specifically those acting on carboxylic ester bonds. Some exceptions include an esterase with beta-lactamase like structure (PDB 1ci8). The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases.
Carboxylesterase is an enzyme that is capable of hydrolyzing a wide variety of carboxylic acid esters. Although its metabolic function is unclear, the enzyme is widely distributed in nature, being especially common in mammalian liver. Carboxylesterase belongs to the class of serine hydrolases which includes Chymotrypsin and Acetylcholinesterase.
The systematic name of this enzyme class is carboxylic-ester hydrolase. Examples of carboxyesterases include:
- butyrate esterase,
- butyryl esterase,
- carboxyl ester hydrolase,
- carboxylate esterase,
- carboxylic acid esterase,
- carboxylic esterase,
- esterase A,
- esterase B,
- esterase D,
- methylbutyrate esterase,
- nonspecific carboxylesterase,
- procaine esterase,
- propionyl esterase,
- serine esterase,
- triacetin esterase,
- vitamin A esterase, and
- cocaine esterase.
The last enzyme also participates in alkaloid biosynthesis.
Humans genes that encode carboxylesterase enzymes include:
As of late 2007, 38 structures have been solved for this class of enzymes, with PDB accession codes 1AUO, 1AUR, 1CI8, 1CI9, 1EVQ, 1JJI, 1K4Y, 1L7Q, 1L7R, 1MX1, 1MX5, 1MX9, 1QZ3, 1R1D, 1TQH, 1U4N, 1YA4, 1YA8, 1YAH, 1YAJ, 2C7B, 2DQY, 2DQZ, 2DR0, 2FJ0, 2H1I, 2H7C, 2HM7, 2HRQ, 2HRR, 2JEY, 2JEZ, 2JF0, 2O7R, 2O7V, 2OGS, 2OGT, and 2R11.
- Augusteyn RC, de Jersey J, Webb EC, Zerner B (1969). "On the homology of the active-site peptides of liver carboxylesterases". Biochim. Biophys. Acta. 171 (1): 128–37. PMID 4884138.
- Barker DL, Jencks WP (1969). "Pig liver esterase. Physical properties". Biochemistry. 8 (10): 3879–89. doi:10.1021/bi00838a001. PMID 4981346.
- Bertram J, Krisch K (1969). "Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney". Eur. J. Biochem. 11 (1): 122–6. doi:10.1111/j.1432-1033.1969.tb00748.x. PMID 5353595.
- BURCH J (1954). "The purification and properties of horse liver esterase". Biochem. J. 58 (3): 415–26. PMC 1269916. PMID 13208632.
- Horgan DJ, Stoops JK, Webb EC, Zerner B (1969). "Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase". Biochemistry. 8 (5): 2000–6. doi:10.1021/bi00833a033. PMID 5785220.
- Malhotra OP and Philip G (1966). "Specificity of goat intestinal esterase". Biochem. Z. 346: 386–402.
- Mentlein R, Schumann M, Heymann E (1984). "Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes". Arch. Biochem. Biophys. 234 (2): 612–21. doi:10.1016/0003-9861(84)90311-4. PMID 6208846.
- Runnegar MT, Scott K, Webb EC, Zerner B (1969). "Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase". Biochemistry. 8 (5): 2013–8. doi:10.1021/bi00833a035. PMID 5785222.
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