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carboxylesterase

{{Short description|Class of enzymes}}

{{infobox enzyme

| Name = carboxylesterase

| EC_number = 3.1.1.1

| CAS_number = 9016-18-6

| GO_code = 0004091

| image =

| width =

| caption =

}}

The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:{{cite journal|last1=Aranda|first1=Juan|last2=Cerqueira|first2=N. M. F. S. A.|last3=Fernandes|first3=P.A.|last4=Roca|first4=M.|last5=Tuñon|first5=I.|last6=Ramos|first6=M. J.|title=The Catalytic Mechanism of Carboxylesterases. A Computational Study.|journal=Biochemistry|date=2014|volume=53|issue=36|pages=5820–5829|doi=10.1021/bi500934j|pmid=25101647}}

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

Most enzymes from this group are serine hydrolases belonging to the superfamily of proteins with α/β hydrolase fold. Some exceptions include an esterase with β-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 essential polyunsaturated fatty acid arachidonic acid (AA C20H32O2; 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor.{{Cite web |last=PubChem |title=Arachidonic acid |url=https://pubchem.ncbi.nlm.nih.gov/compound/444899 |access-date=2022-11-24 |website=pubchem.ncbi.nlm.nih.gov |language=en}}

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

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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.{{cite journal |vauthors=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 | title = Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins | journal = Mamm. Genome | volume = 21 | issue = 9–10 | pages = 427–41 | year = 2010 | pmid = 20931200 | pmc = 3127206 | doi = 10.1007/s00335-010-9284-4 }}

References

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Further reading

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  • {{cite journal |vauthors=Augusteyn RC, de Jersey J, Webb EC, Zerner B | date = 1969 | title = On the homology of the active-site peptides of liver carboxylesterases | journal = Biochim. Biophys. Acta | volume = 171 | pages = 128–37 | pmid = 4884138 | issue = 1 | doi=10.1016/0005-2744(69)90112-0}}
  • {{cite journal |vauthors=Barker DL, Jencks WP | date = 1969 | title = Pig liver esterase. Physical properties | journal = Biochemistry | volume = 8 | pages = 3879–89 | pmid = 4981346 | doi = 10.1021/bi00838a001 | issue = 10 }}
  • {{cite journal |vauthors=Bertram J, Krisch K | date = 1969 | title = Hydrolysis of vitamin A acetate by unspecific carboxylesterases from liver and kidney | journal = Eur. J. Biochem. | volume = 11 | pages = 122–6 | pmid = 5353595 | doi = 10.1111/j.1432-1033.1969.tb00748.x | issue = 1 | doi-access = free }}
  • {{cite journal | author = BURCH J | date = 1954 | title = The purification and properties of horse liver esterase | journal = Biochem. J. | volume = 58 | pages = 415–26 | pmid = 13208632 | issue = 3 | pmc = 1269916 | doi = 10.1042/bj0580415 }}
  • {{cite journal |vauthors=Horgan DJ, Stoops JK, Webb EC, Zerner B | date = 1969 | title = Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase | journal = Biochemistry | volume = 8 | pages = 2000–6 | pmid = 5785220 | doi = 10.1021/bi00833a033 | issue = 5 }}
  • {{cite journal |vauthors=Malhotra OP, Philip G| date = 1966 | title = Specificity of goat intestinal esterase | journal = Biochem. Z. | volume = 346 | pages = 386–402 }}
  • {{cite journal |vauthors=Mentlein R, Schumann M, Heymann E | date = 1984 | title = Comparative chemical and immunological characterization of five lipolytic enzymes (carboxylesterases) from rat liver microsomes | journal = Arch. Biochem. Biophys. | volume = 234 | pages = 612–21 | pmid = 6208846 | doi = 10.1016/0003-9861(84)90311-4 | issue = 2 }}
  • {{cite journal |vauthors=Runnegar MT, Scott K, Webb EC, Zerner B | date = 1969 | title = Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase | journal = Biochemistry | volume = 8 | pages = 2013–8 | pmid = 5785222 | doi = 10.1021/bi00833a035 | issue = 5 }}

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{{Esterases}}

{{Enzymes}}

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Category:EC 3.1.1