carboxyesterase

カルボキシエステラーゼ

関

carboxylesterase、carboxylic ester hydrolase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/04 04:04:19」(JST)

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carboxylesterase
Identifiers
EC number	3.1.1.1
CAS number	9016-18-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

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

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 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

• acetylcholinesterase
• ali-esterase,
• B-esterase,
• butyrate esterase,
• butyryl esterase,
• carboxylesterase 1
• carboxylesterase 2
• carboxylesterase 3
• esterase A,
• esterase B,
• esterase D,
• methylbutyrase,
• methylbutyrate esterase,
• monobutyrase,
• procaine esterase,
• propionyl esterase,
• triacetin esterase,
• vitamin A esterase, and
• cocaine esterase

The last enzyme also participates in alkaloid biosynthesis.

Genes

Humans genes that encode carboxylesterase enzymes include:

• CES1
• CES2
• CES3
• CES4
• CES7
• CES8

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

References

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. 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. 

English Journal

• The carboxylesterase/cholinesterase gene family in invertebrate deuterostomes.

• Johnson G, Moore SW.AbstractCarboxylesterase/cholinesterase family members are responsible for controlling the nerve impulse, detoxification and various developmental functions, and are a major target of pesticides and chemical warfare agents. Comparative structural analysis of these enzymes is thus important. The invertebrate deuterostomes (phyla Echinodermata and Hemichordata and subphyla Urochordata and Cephalochordata) lie in the transition zone between invertebrates and vertebrates, and are thus of interest to the study of evolution. Here we have investigated the carboxylesterase/cholinesterase gene family in the sequenced genomes of Strongylocentrotus purpuratus (Echinodermata), Saccoglossus kowalevskii (Hemichordata), Ciona intestinalis (Urochordata) and Branchiostoma floridae (Cephalochordata), using sequence analysis of the catalytic apparatus and oligomerisation domains, and phylogenetic analysis. All four genomes show blurring of structural boundaries between cholinesterases and carboxylesterases, with many intermediate enzymes. Non-enzymatic proteins are well represented. The Saccoglossus and Branchiostoma genomes show evidence of extensive gene duplication and retention. There is also evidence of domain shuffling, resulting in multidomain proteins consisting either of multiple carboxylesterase domains, or of carboxylesterase/cholinesterase domains linked to other domains, including RING finger, chitin-binding, immunoglobulin, fibronectin type 3, CUB, cysteine-rich-Frizzled, caspase activation and 7tm-1, amongst others. Such gene duplication and domain shuffling in the carboxylesterase/cholinesterase family appears to be unique to the invertebrate deuterostomes, and we hypothesise that these factors may have contributed to the evolution of the morphological complexity, particularly of the nervous system and neural crest, of the vertebrates.
• Comparative biochemistry and physiology. Part D, Genomics & proteomics.Comp Biochem Physiol Part D Genomics Proteomics.2012 Jun;7(2):83-93. Epub 2011 Nov 28.
• Carboxylesterase/cholinesterase family members are responsible for controlling the nerve impulse, detoxification and various developmental functions, and are a major target of pesticides and chemical warfare agents. Comparative structural analysis of these enzymes is thus important. The invertebrate
• PMID 22210164

• In vivo studies on inhibition and recovery of B-esterase activities in Biomphalaria glabrata exposed to azinphos-methyl: analysis of enzyme, substrate and tissue dependence.

• Kristoff G, Barrionuevo DC, Cacciatore LC, Guerrero NR, Cochón AC.SourceDepartamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Nuñez, 1428 Buenos Aires, Argentina.
• Aquatic toxicology (Amsterdam, Netherlands).Aquat Toxicol.2012 May 15;112-113:19-26. Epub 2012 Jan 27.
• Cholinesterases and carboxylesterases belong to the group of B-esterases, the serine superfamily of esterases that are inhibited by organophosphorus compounds. It is now generally accepted that before using the B-esterases as biomarkers of exposure to organophosphorus and carbamates in a given speci
• PMID 22360939

Japanese Journal

• β-ナフチルアセテートを使った食品等の昆虫類異物検査

• ペストロジー 20(1), 25-27, 2005-06-30
• NAID 110007328485

• The Transmembrane Region of Microsomal Cytochrome P450 Identified as the Endoplasmic Reticulum Retention Signal.

• The Journal of Biochemistry 116(1), 164-175, 1994
• NAID 130003532200

• 2-ナフチルラウリン酸を基質にする血清リパーゼ活性のアンペロメトリック測定

• 分析化学 42(8), 491-495, 1993-08-05
• NAID 110002906606

Related Pictures

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★リンクテーブル★

リンク元	「carboxylic ester hydrolase」「カルボキシエステラーゼ」「carboxylesterase」

「carboxylic ester hydrolase」

　　[★]

カルボキシルエステル加水分解酵素、カルボキシルエステルヒドロラーゼ

関

carboxyesterase、carboxylesterase

「カルボキシエステラーゼ」

　　[★]

英

carboxyesterase、carboxylesterase

関

カルボキシルエステルヒドロラーゼ

「carboxylesterase」

　　[★]

カルボキシエステラーゼ

関

carboxyesterase、carboxylic ester hydrolase