Carboxylesterase

In enzymology, a carboxylesterase or carboxylic-ester hydrolase (EC 3.1.1.1) is an enzyme that catalyzes a chemical reaction of the form

a carboxylic ester + H2O an alcohol + a carboxylate
carboxylesterase
Identifiers
EC number3.1.1.1
CAS number9016-18-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are carboxylic ester and H2O, whereas its two products are alcohol and carboxylate.[1]

Most enzymes from this group are serine hydrolases belonging to the superfamily of proteins with alpha/beta hydrolase fold. Some exceptions include an esterase with beta-lactamase like structure (PDB: 1ci8​).

Carboxylesterases are widely distributed in nature, and are common in mammalian liver. Many participate in phase I metabolism of xenobiotics such as toxins or drugs; the resulting carboxylates are then conjugated by other enzymes to increase solubility and eventually excreted.

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.

Examples

The last enzyme also participates in alkaloid biosynthesis.

Genes

Humans genes that encode carboxylesterase enzymes include:

An approved nomenclature has been established for the five mammalian carboxylesterase gene families.[2]

gollark: Yes.
gollark: And obviously macrons.
gollark: As well as `call/cc`.
gollark: Macron obviously has full stack frame inspection capabilities.
gollark: It has `call/cc`.

References
  1. Aranda, Juan; Cerqueira, N. M. F. S. A.; Fernandes, P.A.; Roca, M.; Tuñon, I.; Ramos, M. J. (2014). "The Catalytic Mechanism of Carboxylesterases. A Computational Study". Biochemistry. 53 (36): 5820–5829. doi:10.1021/bi500934j. PMID 25101647.
  2. Holmes RS, Wright MW, Laulederkind SJ, Cox LA, Hosokawa M, Imai T, Ishibashi S, Lehner R, Miyazaki M, Perkins EJ, Potter PM, Redinbo MR, Robert J, Satoh T, Yamashita T, Yan B, Yokoi T, Zechner R, Maltais LJ (2010). "Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins". Mamm. Genome. 21 (9–10): 427–41. doi:10.1007/s00335-010-9284-4. PMC 3127206. PMID 20931200.

Further reading
  • 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. doi:10.1016/0005-2744(69)90112-0. 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. doi:10.1042/bj0580415. 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, 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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