Carboxylesterase

From Wikipedia, the free encyclopedia

In enzymology, a carboxylesterase (EC 3.1.1.1) is an enzyme that catalyzes the chemical reaction

a carboxylic ester + H₂O $\rightleftharpoons$ an alcohol + a carboxylate

Thus, the two substrates of this enzyme are carboxylic ester and H₂O, whereas its two products are alcohol and 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.

The systematic name of this enzyme class is carboxylic-ester hydrolase. Examples of of carboxyesterases include ali-esterase, B-esterase, monobutyrase, 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, and cocaine esterase. The last enzyme participates in alkaloid biosynthesis.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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.

[edit] References

IUBMB entry for 3.1.1.1
BRENDA references for 3.1.1.1 (Recommended.)
PubMed references for 3.1.1.1
PubMed Central references for 3.1.1.1
Google Scholar references for 3.1.1.1
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: 128–37. PMID 4884138.
Barker DL, Jencks WP (1969). "Pig liver esterase. Physical properties". Biochemistry. 8: 3879–89. PMID 4981346.
Bertram J, Krisch K (1969). "Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney". Eur. J. Biochem. 11: 122–6. PMID 5353595.
BURCH J (1954). "The purification and properties of horse liver esterase". Biochem. J. 58: 415–26. 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: 2000–6. 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: 612–21. 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: 2013–8. PMID 5785222.