Caspase 12: Difference between revisions

CASP12
Identifiers
Aliases	CASP12, CASP-12, CASP12P1, caspase 12 (gene/pseudogene), caspase 12, Caspase-12, Caspase_12, IPR035713
External IDs	OMIM: 608633; MGI: 1312922; GeneCards: CASP12; OMA:CASP12 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	104,898,670 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	5,373,032 bp
RNA expression pattern
	Top expressed in
	testicle; ; right lung; ; left ovary; ; gastric mucosa; ; ascending aorta; ; Descending thoracic aorta; ; popliteal artery; ; tibial arteries; ; left coronary artery; ; right ovary;
	Top expressed in
	temporal muscle; ; tunica media of zone of aorta; ; sternocleidomastoid muscle; ; lumbar spinal ganglion; ; triceps brachii muscle; ; intercostal muscle; ; uterus; ; carotid body; ; ascending aorta; ; semi-lunar valve;
	More reference expression data
	n/a
Gene ontology
Molecular function	cysteine-type endopeptidase activity involved in apoptotic process; cysteine-type peptidase activity; cysteine-type endopeptidase activity; cysteine-type endopeptidase activity involved in apoptotic signaling pathway;
Cellular component	NLRP3 inflammasome complex; AIM2 inflammasome complex; IPAF inflammasome complex; endoplasmic reticulum; cytoplasm;
Biological process	regulation of apoptotic process; regulation of inflammatory response; proteolysis; execution phase of apoptosis; apoptotic process; activation of cysteine-type endopeptidase activity involved in apoptotic process; apoptotic signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	100506742
	12364
	ENSG00000204403
	ENSMUSG00000025887
	Q6UXS9
	O08736
	NM_001191016
	NM_009808
	NP_001177945
	NP_033938
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 07:46, 7 July 2024

Caspase 12 is a protein that in humans is encoded by the CASP12 gene. The protein belongs to a family of enzymes called caspases which cleave their substrates at C-terminal aspartic acid residues. It is closely related to caspase 1 and other members of the caspase family, known as inflammatory caspases, which process and activate inflammatory cytokines such as interleukin 1 and interleukin 18.

Gene

It is found on chromosome 11 in humans in a locus with other inflammatory caspases.^[5] CASP12 orthologs^[6] have been identified in numerous mammals for which complete genome data are available.

Clinical significance

The CASP12 gene is subject to polymorphism, which can generate a full-length caspase protein (Csp12L) or an inactive truncated form (Csp12S). The functional form appears to be confined to people of African descent and is linked with susceptibility to sepsis; people carrying the functional gene have decreased responses to bacterial molecules such as lipopolysaccharide (LPS).^[7]^[8]

A study in May 2009 by McGill University Health Centre has suggested that estrogen may serve to block the production of caspase-12, resulting in a stronger inflammatory reaction to bacterial pathogens. The trials were carried out on laboratory mice which had been implanted with the human caspase-12 gene.^[9]^[10]^[11]

The inactive truncated form (Csp12S) of the CASP12 gene was spread and nearly fixed in non-African populations due to positive selection beginning perhaps 60–100 thousand years ago. Its selective advantage is thought to be sepsis resistance in populations that experienced more infectious diseases as population sizes and densities increased.^[12]^[13]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000204403 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025887 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Fischer H, Koenig U, Eckhart L, Tschachler E (2002). "Human caspase 12 has acquired deleterious mutations". Biochem. Biophys. Res. Commun. 293 (2): 722–6. doi:10.1016/S0006-291X(02)00289-9. PMID 12054529.
^ "OrthoMaM phylogenetic marker: CASP12 coding sequence".^{[permanent dead link‍]}
^ Saleh M, Vaillancourt JP, Graham RK, Huyck M, Srinivasula SM, Alnemri ES, Steinberg MH, Nolan V, Baldwin CT, Hotchkiss RS, Buchman TG, Zehnbauer BA, Hayden MR, Farrer LA, Roy S, Nicholson DW (2004). "Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms". Nature. 429 (6987): 75–9. Bibcode:2004Natur.429...75S. doi:10.1038/nature02451. PMID 15129283.
^ Saleh, Maya Mathison; John C. Wolinski; Melissa K. Bensinger; Steve J. Fitzgerald; Patrick Droin; Nathalie Ulevitch; Richard J. Green; Douglas R. Nicholson; Donald W. (2006). "Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice". Nature. 440 (7087): 1064–1068. Bibcode:2006Natur.440.1064S. doi:10.1038/nature04656. PMID 16625199. S2CID 4321520. (Erratum: doi:10.1038/nature04656, PMID 16625199)
^ Yeretssian G, Doiron K, Shao W, Leavitt BR, Hayden MR, Nicholson DW, Saleh M (May 2009). "Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection". Proc. Natl. Acad. Sci. U.S.A. 106 (22): 9016–20. Bibcode:2009PNAS..106.9016Y. doi:10.1073/pnas.0813362106. PMC 2690057. PMID 19447924.
^ "Man flu: real or myth?". Health. NHS UK. 18 May 2009. Archived from the original on 16 February 2010. Retrieved 23 May 2009.
^ "Women 'fight off disease better'". Health. BBC News. 13 May 2009. Retrieved 13 May 2009.
^ Xue, Yali; Daly, Allan; Yngvadottir, Bryndis; Liu, Mengning; Coop, Graham; Kim, Yuseob; Sabeti, Pardis; Chen, Yuan; Stalker, Jim; Huckle, Elizabeth; Burton, John; Leonard, Steven; Rogers, Jane; Tyler-Smith, Chris (2006). "Spread of an Inactive Form of Caspase-12 in Humans Is Due to Recent Positive Selection". The American Journal of Human Genetics. 78 (4): 659–670. doi:10.1086/503116. PMC 1424700. PMID 16532395.
^ Wang, Xiaoxia; Grus, Wendy E.; Zhang, Jianzhi (2006). "Gene Losses during Human Origins". PLOS Biology. 4 (3): e52. doi:10.1371/journal.pbio.0040052. PMC 1361800. PMID 16464126.

External links

The MEROPS online database for peptidases and their inhibitors: C14.013 Archived 6 September 2005 at the Wayback Machine

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000204403 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025887 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Fischer H, Koenig U, Eckhart L, Tschachler E (2002). "Human caspase 12 has acquired deleterious mutations". Biochem. Biophys. Res. Commun. 293 (2): 722–6. doi:10.1016/S0006-291X(02)00289-9. PMID 12054529.

[OrthoMaM-6] "OrthoMaM phylogenetic marker: CASP12 coding sequence".^{[permanent dead link‍]}

[7] Saleh M, Vaillancourt JP, Graham RK, Huyck M, Srinivasula SM, Alnemri ES, Steinberg MH, Nolan V, Baldwin CT, Hotchkiss RS, Buchman TG, Zehnbauer BA, Hayden MR, Farrer LA, Roy S, Nicholson DW (2004). "Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms". Nature. 429 (6987): 75–9. Bibcode:2004Natur.429...75S. doi:10.1038/nature02451. PMID 15129283.

[8] Saleh, Maya Mathison; John C. Wolinski; Melissa K. Bensinger; Steve J. Fitzgerald; Patrick Droin; Nathalie Ulevitch; Richard J. Green; Douglas R. Nicholson; Donald W. (2006). "Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice". Nature. 440 (7087): 1064–1068. Bibcode:2006Natur.440.1064S. doi:10.1038/nature04656. PMID 16625199. S2CID 4321520. (Erratum: doi:10.1038/nature04656, PMID 16625199)

[pmid19447924-9] Yeretssian G, Doiron K, Shao W, Leavitt BR, Hayden MR, Nicholson DW, Saleh M (May 2009). "Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection". Proc. Natl. Acad. Sci. U.S.A. 106 (22): 9016–20. Bibcode:2009PNAS..106.9016Y. doi:10.1073/pnas.0813362106. PMC 2690057. PMID 19447924.

[urlNHS-10] "Man flu: real or myth?". Health. NHS UK. 18 May 2009. Archived from the original on 16 February 2010. Retrieved 23 May 2009.

[urlBBC-11] "Women 'fight off disease better'". Health. BBC News. 13 May 2009. Retrieved 13 May 2009.

[12] Xue, Yali; Daly, Allan; Yngvadottir, Bryndis; Liu, Mengning; Coop, Graham; Kim, Yuseob; Sabeti, Pardis; Chen, Yuan; Stalker, Jim; Huckle, Elizabeth; Burton, John; Leonard, Steven; Rogers, Jane; Tyler-Smith, Chris (2006). "Spread of an Inactive Form of Caspase-12 in Humans Is Due to Recent Positive Selection". The American Journal of Human Genetics. 78 (4): 659–670. doi:10.1086/503116. PMC 1424700. PMID 16532395.

[13] Wang, Xiaoxia; Grus, Wendy E.; Zhang, Jianzhi (2006). "Gene Losses during Human Origins". PLOS Biology. 4 (3): e52. doi:10.1371/journal.pbio.0040052. PMC 1361800. PMID 16464126.

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+{{Short description|Protein found in humans}}
-{{Use dmy dates|date=May 2013}}
+{{Use dmy dates|date=September 2022}}
-{{infobox protein
+{{Infobox gene}}
-| Name = caspase 12
+'''Caspase 12''' is a [[protein]] that in humans is encoded by the ''CASP12'' [[gene]]. The protein belongs to a family of [[enzyme]]s called [[caspase]]s which cleave their [[Substrate (biochemistry)|substrate]]s at [[C-terminal]] [[aspartic acid]] residues.  It is closely related to [[caspase 1]] and other members of the caspase family, known as inflammatory caspases, which process and activate inflammatory [[cytokine]]s such as [[interleukin 1]] and [[interleukin 18]].
-| caption =
-| image =
-| width = 240px
-| HGNCid = 19004
-| Symbol = CASP12
-| AltSymbols = CASP12P1
-| EntrezGene = 120329
-| OMIM = 608633
-| RefSeq = NR_000035
-| UniProt = Q6UXS9
-| PDB =
-| ECnumber =
-| Chromosome = 11
-| Arm = q
-| Band = 22.3
-| LocusSupplementaryData =
-}}
-'''Caspase 12''' is a [[protein]] that belongs to a family of [[enzyme]]s called [[caspase]]s which cleave their [[Substrate (biochemistry)|substrate]]s at [[C-terminal]] [[aspartic acid]] residues.  It is closely related to [[caspase 1]] and other members of the caspase family, known as inflammatory caspases, which process and activate inflammatory [[cytokine]]s such as [[interleukin 1]] and [[interleukin 18]].
 == Gene ==
-It is found on [[chromosome 23]] in cows in a [[Locus (genetics)|locus]] with other inflammatory caspases.<ref>{{cite journal |author=Fischer H, Koenig U, Eckhart L, Tschachler E |title=Human caspase 12 has acquired deleterious mutations |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue=2 |pages=722–6 |year=2002 |pmid=12054529 |doi=10.1016/S0006-291X(02)00289-9}}</ref>
+It is found on [[chromosome 11]] in humans in a [[Locus (genetics)|locus]] with other inflammatory caspases.<ref>{{cite journal |vauthors=Fischer H, Koenig U, Eckhart L, Tschachler E |title=Human caspase 12 has acquired deleterious mutations |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue=2 |pages=722–6 |year=2002 |pmid=12054529 |doi=10.1016/S0006-291X(02)00289-9}}</ref>
-''CASP12'' [[orthologs]]<ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: CASP12 coding sequence | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000204403_CASP12.xml }}</ref> have been identified in numerous [[mammals]] for which complete genome data are available.
+''CASP12'' [[orthologs]]<ref name="OrthoMaM">{{cite web|title=OrthoMaM phylogenetic marker: CASP12 coding sequence |url=http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000204403_CASP12.xml }}{{dead link|date=November 2016 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> have been identified in numerous [[mammal]]s for which complete genome data are available.
 == Clinical significance ==
-The CASP12 [[gene]] is subject to [[Polymorphism (biology)|polymorphism]], which can generate a full length caspase protein (Csp12L) or an inactive truncated form (Csp12S). The functional form appears to be confined to people of [[Ethnic groups of Africa|African]] descent and is linked with susceptibility to [[sepsis]]; people carrying the functional gene have decreased responses to bacterial molecules such as [[lipopolysaccharide]] (LPS).<ref>{{cite journal |author=Saleh M, Vaillancourt JP, Graham RK, Huyck M, Srinivasula SM, Alnemri ES, Steinberg MH, Nolan V, Baldwin CT, Hotchkiss RS, Buchman TG, Zehnbauer BA, Hayden MR, Farrer LA, Roy S, Nicholson DW |title=Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms |journal=Nature |volume=429 |issue=6987 |pages=75–9 |year=2004 |pmid=15129283 |doi=10.1038/nature02451}}</ref><ref>{{cite journal |author=Saleh, Maya Mathison, John C. Wolinski, Melissa K. Bensinger, Steve J. Fitzgerald, Patrick Droin, Nathalie Ulevitch, Richard J. Green, Douglas R. Nicholson, Donald W. |title=Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice |journal=Nature |volume=440 |issue=7087 |pages=1064–1068 |year=2006 |doi=10.1038/nature04656 |pmid=16625199 }}</ref>
+The CASP12 [[gene]] is subject to [[Polymorphism (biology)|polymorphism]], which can generate a full-length caspase protein (Csp12L) or an inactive truncated form (Csp12S). The functional form appears to be confined to people of [[Ethnic groups of Africa|African]] descent and is linked with susceptibility to [[sepsis]]; people carrying the functional gene have decreased responses to bacterial molecules such as [[lipopolysaccharide]] (LPS).<ref>{{cite journal |vauthors=Saleh M, Vaillancourt JP, Graham RK, Huyck M, Srinivasula SM, Alnemri ES, Steinberg MH, Nolan V, Baldwin CT, Hotchkiss RS, Buchman TG, Zehnbauer BA, Hayden MR, Farrer LA, Roy S, Nicholson DW |title=Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms |journal=Nature |volume=429 |issue=6987 |pages=75–9 |year=2004 |pmid=15129283 |doi=10.1038/nature02451|bibcode=2004Natur.429...75S |doi-access=free }}</ref><ref>{{cite journal |author=Saleh, Maya Mathison |author2=John C. Wolinski |author3=Melissa K. Bensinger |author4=Steve J. Fitzgerald |author5=Patrick Droin |author6=Nathalie Ulevitch |author7=Richard J. Green |author8=Douglas R. Nicholson |author9=Donald W. |title=Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice |journal=Nature |volume=440 |issue=7087 |pages=1064–1068 |year=2006 |doi=10.1038/nature04656 |pmid=16625199 |bibcode=2006Natur.440.1064S |s2cid=4321520 }}{{Erratum|doi=10.1038/nature04656|pmid=16625199|checked=yes}}</ref>
-A study in May 2009 by McGill University Health Centre has suggested that [[estrogen]] may serve to block the production of caspase-12, resulting in a stronger inflammatory reaction to bacterial pathogens. The trials were carried out on laboratory mice which had been implanted with the human caspase-12 gene.<ref name="pmid19447924">{{cite journal | author = Yeretssian G, Doiron K, Shao W, Leavitt BR, Hayden MR, Nicholson DW, Saleh M | title = Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 106| issue = 22| pages = 9016–20|date=May 2009 | pmid = 19447924 | doi = 10.1073/pnas.0813362106 | url = | pmc = 2690057 }}</ref><ref name="urlNHS">{{cite web | url = http://www.nhs.uk/news/2009/05May/Pages/Manflurealormyth.aspx | title =  Man flu: real or myth?  | author = | authorlink = | coauthors = | date = 2009-05-18 | format = | work = Health | publisher = NHS UK | pages = | language = | archiveurl = | archivedate = | quote = }}</ref><ref name="urlBBC">{{cite web | url = http://news.bbc.co.uk/1/hi/health/8047321.stm | title =  Women 'fight off disease better' | author = | authorlink = | coauthors = | date = 2009-05-13 | format = | work = Health | publisher = BBC News | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = 2009-05-13}}</ref>
+A study in May 2009 by McGill University Health Centre has suggested that [[estrogen]] may serve to block the production of caspase-12, resulting in a stronger inflammatory reaction to bacterial pathogens. The trials were carried out on laboratory mice which had been implanted with the human caspase-12 gene.<ref name="pmid19447924">{{cite journal | vauthors = Yeretssian G, Doiron K, Shao W, Leavitt BR, Hayden MR, Nicholson DW, Saleh M | title = Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 106| issue = 22| pages = 9016–20|date=May 2009 | pmid = 19447924 | doi = 10.1073/pnas.0813362106 | pmc = 2690057 | bibcode = 2009PNAS..106.9016Y | doi-access = free }}</ref><ref name="urlNHS">{{cite web | url = http://www.nhs.uk/news/2009/05May/Pages/Manflurealormyth.aspx | title = Man flu: real or myth? | date = 2009-05-18 | work = Health | publisher = NHS UK | access-date = 23 May 2009 | archive-date = 16 February 2010 | archive-url = https://web.archive.org/web/20100216113214/http://www.nhs.uk/news/2009/05May/Pages/Manflurealormyth.aspx | url-status = dead }}</ref><ref name="urlBBC">{{cite web | url = http://news.bbc.co.uk/1/hi/health/8047321.stm | title =  Women 'fight off disease better' | date = 2009-05-13 | work = Health | publisher = BBC News | accessdate = 2009-05-13}}</ref>
-The inactive truncated form (Csp12S) of the CASP12 [[gene]] was spread and nearly fixed in non-African populations due to [[Directional selection|positive selection]] beginning perhaps 60–100 thousand years ago. Its selective advantage is thought to be sepsis resistance in populations that experienced more infectious diseases as population sizes and densities increased.<ref>{{cite journal | url = http://www.sciencedirect.com/science/article/pii/S0002929707637033 | doi=10.1086/503116 | volume=78 | title=Spread of an Inactive Form of Caspase-12 in Humans Is Due to Recent Positive Selection | journal=The American Journal of Human Genetics | pages=659–670 | pmid=16532395 | pmc=1424700}}</ref><ref>{{cite journal | doi = 10.1371/journal.pbio.0040052 | volume=4 | title=Gene Losses during Human Origins | journal=PLoS Biology | pages=e52 | pmid=16464126 | pmc=1361800}}</ref>
+The inactive truncated form (Csp12S) of the CASP12 [[gene]] was spread and nearly fixed in non-African populations due to [[Directional selection|positive selection]] beginning perhaps 60–100 thousand years ago. Its selective advantage is thought to be sepsis resistance in populations that experienced more infectious diseases as population sizes and densities increased.<ref>{{cite journal | doi=10.1086/503116 | volume=78 | issue=4 | title=Spread of an Inactive Form of Caspase-12 in Humans Is Due to Recent Positive Selection | journal=The American Journal of Human Genetics | pages=659–670 | pmid=16532395 | pmc=1424700| year=2006 | last1=Xue | first1=Yali | last2=Daly | first2=Allan | last3=Yngvadottir | first3=Bryndis | last4=Liu | first4=Mengning | last5=Coop | first5=Graham | last6=Kim | first6=Yuseob | last7=Sabeti | first7=Pardis |author7-link=Pardis Sabeti | last8=Chen | first8=Yuan | last9=Stalker | first9=Jim | last10=Huckle | first10=Elizabeth | last11=Burton | first11=John | last12=Leonard | first12=Steven | last13=Rogers | first13=Jane | last14=Tyler-Smith | first14=Chris }}</ref><ref>{{cite journal | doi = 10.1371/journal.pbio.0040052 | volume=4 | issue=3 | title=Gene Losses during Human Origins | journal=PLOS Biology | pages=e52 | pmid=16464126 | pmc=1361800| year=2006 | last1=Wang | first1=Xiaoxia | last2=Grus | first2=Wendy E. | last3=Zhang | first3=Jianzhi | doi-access=free }}</ref>
 ==References==
-{{Reflist|2}}
+{{Reflist}}
 ==External links==
-* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C14.013 C14.013]
+* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C14.013 C14.013] {{Webarchive|url=https://web.archive.org/web/20050906225501/http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C14.013 |date=6 September 2005 }}
 {{Cysteine proteases}}
 {{Enzymes}}
-{{Portal bar|Molecular and Cellular Biology|border=no}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 3.4.22]]
+[[Category:Caspases]]

v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)