MAST2

Protein-coding gene in the species Homo sapiens

MAST2

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

2KQF, 2KYL

Identifiers
Aliases| MAST2, MAST205, MTSSK, microtubule associated serine/threonine kinase 2
External IDs| OMIM: 612257; MGI: 894676; HomoloGene: 7428; GeneCards: MAST2; OMA:MAST2 - orthologs
| Gene location (Human)

Chr.| Chromosome 1 (human)[1]

Band| 1p34.1| Start| 45,786,987 bp[1]
End| 46,036,122 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 4 (mouse)[2]

Band| 4|4 D1| Start| 116,306,762 bp[2]
End| 116,464,183 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* gastrocnemius muscle

* muscle of thigh

* apex of heart

* gastric mucosa

* glutes

* stromal cell of endometrium

* pancreatic ductal cell

* skeletal muscle tissue

* left ventricle

* left testis

| Top expressed in

* neural layer of retina

* muscle of thigh

* internal carotid artery

* right ventricle

* ankle joint

* cardiac muscle tissue of left ventricle

* external carotid artery

* ankle

* digastric muscle

* soleus muscle

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* transferase activity
* nucleotide binding
* protein kinase activity
* phosphatase binding
* microtubule binding
* metal ion binding
* kinase activity
* protein serine/threonine kinase activity
* protein binding
* ATP binding
* magnesium ion binding

Cellular component|

* membrane
* microtubule cytoskeleton
* plasma membrane
* cytoskeleton
* cytoplasm

Biological process|

* intracellular signal transduction
* phosphorylation
* spermatid differentiation
* protein phosphorylation
* cytoskeleton organization
* peptidyl-serine phosphorylation

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

23139

17776

Ensembl| |

ENSG00000086015

ENSMUSG00000003810

UniProt| |

Q6P0Q8

Q60592

RefSeq (mRNA)| |

NM_015112
NM_001319245
NM_001324320
NM_001324321

NM_001042743
NM_008641
NM_001369061
NM_001369062

RefSeq (protein)| |

NP_001306174
NP_001311249
NP_001311250
NP_055927

NP_001036208
NP_032667
NP_001355990
NP_001355991

Location (UCSC)| Chr 1: 45.79 – 46.04 Mb| Chr 4: 116.31 – 116.46 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Microtubule-associated serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the MAST2 gene.[5] The protein encoded by this gene controls TRAF6 and NF-kappaB activity.[6]

## Interactions

[edit]

MAST2 has been shown to interact with PCLKC.[7]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000086015 - Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003810 - 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. ^ "Entrez Gene: MAST2 microtubule associated serine/threonine kinase 2".
6. ^ Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (2004). "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability". J. Biol. Chem. 279 (42): 43675–83\. doi:10.1074/jbc.M404328200. PMID 15308666.43675-83&rft.date=2004&rft_id=info:doi/10.1074/jbc.M404328200&rft_id=info:pmid/15308666&rft.aulast=Xiong&rft.aufirst=H&rft.au=Li,+H&rft.au=Chen,+Y&rft.au=Zhao,+J&rft.au=Unkeless,+JC&rft_id=https://doi.org/10.1074%2Fjbc.M404328200&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
7. ^ Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (July 2002). "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation". Carcinogenesis. 23 (7): 1139–48\. doi:10.1093/carcin/23.7.1139. PMID 12117771.1139-48&rft.date=2002-07&rft_id=info:doi/10.1093/carcin/23.7.1139&rft_id=info:pmid/12117771&rft.aulast=Okazaki&rft.aufirst=N&rft.au=Takahashi,+N&rft.au=Kojima,+S&rft.au=Masuho,+Y&rft.au=Koga,+H&rft_id=https://doi.org/10.1093%2Fcarcin%2F23.7.1139&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">

## Further reading

[edit]

* Walden PD, Cowan NJ (1993). "A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette". Mol. Cell. Biol. 13 (12): 7625–35\. doi:10.1128/mcb.13.12.7625. PMC 364834. PMID 8246979.7625-35&rft.date=1993&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC364834#id-name=PMC&rft_id=info:pmid/8246979&rft_id=info:doi/10.1128/mcb.13.12.7625&rft.aulast=Walden&rft.aufirst=PD&rft.au=Cowan,+NJ&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC364834&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806\. doi:10.1101/gr.6.9.791. PMID 8889548.791-806&rft.date=1996&rft_id=info:doi/10.1101/gr.6.9.791&rft_id=info:pmid/8889548&rft.aulast=Bonaldo&rft.aufirst=MF&rft.au=Lennon,+G&rft.au=Soares,+MB&rft_id=https://doi.org/10.1101%2Fgr.6.9.791&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Walden PD, Millette CF (1996). "Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis". Biol. Reprod. 55 (5): 1039–44\. doi:10.1095/biolreprod55.5.1039. PMID 8902215.1039-44&rft.date=1996&rft_id=info:doi/10.1095/biolreprod55.5.1039&rft_id=info:pmid/8902215&rft.aulast=Walden&rft.aufirst=PD&rft.au=Millette,+CF&rft_id=https://doi.org/10.1095%2Fbiolreprod55.5.1039&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86\. doi:10.1093/dnares/5.5.277. PMID 9872452.277-86&rft.date=1998&rft_id=info:doi/10.1093/dnares/5.5.277&rft_id=info:pmid/9872452&rft.aulast=Nagase&rft.aufirst=T&rft.au=Ishikawa,+K&rft.au=Suyama,+M&rft.au=Kikuno,+R&rft.au=Miyajima,+N&rft.au=Tanaka,+A&rft.au=Kotani,+H&rft.au=Nomura,+N&rft.au=Ohara,+O&rft_id=https://doi.org/10.1093%2Fdnares%2F5.5.277&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Lumeng C, Phelps S, Crawford GE, Walden PD, Barald K, Chamberlain JS (1999). "Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases". Nat. Neurosci. 2 (7): 611–7\. doi:10.1038/10165. PMID 10404183. S2CID 20910888.611-7&rft.date=1999&rft_id=https://api.semanticscholar.org/CorpusID:20910888#id-name=S2CID&rft_id=info:pmid/10404183&rft_id=info:doi/10.1038/10165&rft.aulast=Lumeng&rft.aufirst=C&rft.au=Phelps,+S&rft.au=Crawford,+GE&rft.au=Walden,+PD&rft.au=Barald,+K&rft.au=Chamberlain,+JS&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL (2000). "Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding". Cancer Res. 60 (1): 35–7\. PMID 10646847.35-7&rft.date=2000&rft_id=info:pmid/10646847&rft.aulast=Adey&rft.aufirst=NB&rft.au=Huang,+L&rft.au=Ormonde,+PA&rft.au=Baumgard,+ML&rft.au=Pero,+R&rft.au=Byreddy,+DV&rft.au=Tavtigian,+SV&rft.au=Bartel,+PL&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, Murer H (2001). "Interaction of the type IIa Na/Pi cotransporter with PDZ proteins". J. Biol. Chem. 276 (12): 9206–13\. doi:10.1074/jbc.M008745200. PMID 11099500.9206-13&rft.date=2001&rft_id=info:doi/10.1074/jbc.M008745200&rft_id=info:pmid/11099500&rft.aulast=Gisler&rft.aufirst=SM&rft.au=Stagljar,+I&rft.au=Traebert,+M&rft.au=Bacic,+D&rft.au=Biber,+J&rft.au=Murer,+H&rft_id=https://doi.org/10.1074%2Fjbc.M008745200&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (2002). "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation". Carcinogenesis. 23 (7): 1139–48\. doi:10.1093/carcin/23.7.1139. PMID 12117771.1139-48&rft.date=2002&rft_id=info:doi/10.1093/carcin/23.7.1139&rft_id=info:pmid/12117771&rft.aulast=Okazaki&rft.aufirst=N&rft.au=Takahashi,+N&rft.au=Kojima,+S&rft.au=Masuho,+Y&rft.au=Koga,+H&rft_id=https://doi.org/10.1093%2Fcarcin%2F23.7.1139&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Nakayama M, Kikuno R, Ohara O (2002). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–84\. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.1773-84&rft.date=2002&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC187542#id-name=PMC&rft_id=info:pmid/12421765&rft_id=info:doi/10.1101/gr.406902&rft.aulast=Nakayama&rft.aufirst=M&rft.au=Kikuno,+R&rft.au=Ohara,+O&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC187542&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics. 4 (2): 339–46\. doi:10.1002/pmic.200300528. PMID 14760703. S2CID 8868600.339-46&rft.date=2004&rft_id=https://api.semanticscholar.org/CorpusID:8868600#id-name=S2CID&rft_id=info:pmid/14760703&rft_id=info:doi/10.1002/pmic.200300528&rft.aulast=Navarro-Lérida&rft.aufirst=I&rft.au=Martínez+Moreno,+M&rft.au=Roncal,+F&rft.au=Gavilanes,+F&rft.au=Albar,+JP&rft.au=Rodríguez-Crespo,+I&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Zhou H, Xiong H, Li H, Plevy SE, Walden PD, Sassaroli M, Prestwich GD, Unkeless JC (2004). "Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation". J. Immunol. 172 (4): 2559–68\. doi:10.4049/jimmunol.172.4.2559. PMID 14764729. S2CID 85692192.2559-68&rft.date=2004&rft_id=https://api.semanticscholar.org/CorpusID:85692192#id-name=S2CID&rft_id=info:pmid/14764729&rft_id=info:doi/10.4049/jimmunol.172.4.2559&rft.aulast=Zhou&rft.aufirst=H&rft.au=Xiong,+H&rft.au=Li,+H&rft.au=Plevy,+SE&rft.au=Walden,+PD&rft.au=Sassaroli,+M&rft.au=Prestwich,+GD&rft.au=Unkeless,+JC&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16\. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.707-16&rft.date=2004&rft_id=https://api.semanticscholar.org/CorpusID:27764390#id-name=S2CID&rft_id=info:pmid/15146197&rft_id=info:doi/10.1038/nbt971&rft.aulast=Brandenberger&rft.aufirst=R&rft.au=Wei,+H&rft.au=Zhang,+S&rft.au=Lei,+S&rft.au=Murage,+J&rft.au=Fisk,+GJ&rft.au=Li,+Y&rft.au=Xu,+C&rft.au=Fang,+R&rft.au=Guegler,+K&rft.au=Rao,+MS&rft.au=Mandalam,+R&rft.au=Lebkowski,+J&rft.au=Stanton,+LW&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (2004). "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability". J. Biol. Chem. 279 (42): 43675–83\. doi:10.1074/jbc.M404328200. PMID 15308666.43675-83&rft.date=2004&rft_id=info:doi/10.1074/jbc.M404328200&rft_id=info:pmid/15308666&rft.aulast=Xiong&rft.aufirst=H&rft.au=Li,+H&rft.au=Chen,+Y&rft.au=Zhao,+J&rft.au=Unkeless,+JC&rft_id=https://doi.org/10.1074%2Fjbc.M404328200&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48\. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.635-48&rft.date=2006&rft_id=https://api.semanticscholar.org/CorpusID:7827573#id-name=S2CID&rft_id=info:pmid/17081983&rft_id=info:doi/10.1016/j.cell.2006.09.026&rft.aulast=Olsen&rft.aufirst=JV&rft.au=Blagoev,+B&rft.au=Gnad,+F&rft.au=Macek,+B&rft.au=Kumar,+C&rft.au=Mortensen,+P&rft.au=Mann,+M&rft_id=https://doi.org/10.1016%2Fj.cell.2006.09.026&rfr_id=info:sid/en.wikipedia.org:MAST2" class="Z3988">
* Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

* v
* t
* e

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

| Non-specific serine/threonine protein kinases (EC 2.7.11.1)|

* LATS1
* LATS2
* MAST1
* MAST2
* STK38
* STK38L
* CIT
* ROCK1
* SGK
* SGK2
* SGK3
* Protein kinase B
* AKT1
* AKT2
* AKT3
* Ataxia telangiectasia mutated
* mTOR
* EIF-2 kinases
* PKR
* HRI
* EIF2AK3
* EIF2AK4
* Wee1
* WEE1

|

Pyruvate dehydrogenase kinase (EC 2.7.11.2)|

* PDK1
* PDK2
* PDK3
* PDK4

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)|

* AMP-activated protein kinase α
* PRKAA1
* PRKAA2
* β
* PRKAB1
* PRKAB2
* γ
* PRKAG1
* PRKAG2
* PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)|

* BCKDK
* BCKDHA
* BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)|

* IDH2
* IDH3A
* IDH3B
* IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)|

* STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)|

* Aurora kinase
* Aurora A kinase
* Aurora B kinase
* Aurora C kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)|

* FASTK
* STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)|

* -

IκB kinase (EC 2.7.11.10)|

* CHUK
* IKK2
* TBK1
* IKBKE
* IKBKG
* IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)|

* Protein kinase A
* PRKACG
* PRKACB
* PRKACA
* PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)|

* Protein kinase G
* PRKG1

Protein kinase C (EC 2.7.11.13)|

* Protein kinase C
* Protein kinase Cζ
* PKC alpha
* PRKCB1
* PRKCD
* PRKCE
* PRKCH
* PRKCG
* PRKCI
* PRKCQ
* Protein kinase N1
* PKN2
* PKN3

Rhodopsin kinase (EC 2.7.11.14)|

* Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)|

* Beta adrenergic receptor kinase
* Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)|

* GRK4
* GRK5
* GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)|

* BRSK2
* CAMK1
* CAMK1A
* CAMK1B
* CAMK1D
* CAMK1G
* CAMK2
* CAMK2A
* CAMK2B
* CAMK2D
* CAMK2G
* CAMK4
* MLCK
* CASK
* CHEK1
* CHEK2
* DAPK1
* DAPK2
* DAPK3
* STK11
* MAPKAPK2
* MAPKAPK3
* MAPKAPK5
* MARK1
* MARK2
* MARK3
* MARK4
* MELK
* MKNK1
* MKNK2
* NUAK1
* NUAK2
* OBSCN
* PASK
* PHKG1
* PHKG2
* PIM1
* PIM2
* PKD1
* PRKD2
* PRKD3
* PSKH1
* SNF1LK2
* KIAA0999
* STK40
* SNF1LK
* SNRK
* SPEG
* TSSK2
* Kalirin
* TRIB1
* TRIB2
* TRIB3
* TRIO
* Titin
* DCLK1

Myosin light-chain kinase (EC 2.7.11.18)|

* MYLK
* MYLK2
* MYLK3
* MYLK4

Phosphorylase kinase (EC 2.7.11.19)|

* PHKA1
* PHKA2
* PHKB
* PHKG1
* PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)|

* EEF2K
* STK19

Polo kinase (EC 2.7.11.21)|

* PLK1
* PLK2
* PLK3
* PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

| Polo kinase (EC 2.7.11.21)|

* PLK1
* PLK2
* PLK3
* PLK4

|

Cyclin-dependent kinase (EC 2.7.11.22)|

* CDK1
* CDK2
* CDKL2
* CDK3
* CDK4
* CDK5
* CDKL5
* CDK6
* CDK7
* CDK8
* CDK9
* CDK10
* CDK12
* CDC2L5
* PCTK1
* PCTK2
* PCTK3
* PFTK1
* CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)|

* RPS6KA5
* RPS6KA4
* P70S6 kinase
* P70-S6 Kinase 1
* RPS6KB2
* RPS6KA2
* RPS6KA3
* RPS6KA1
* RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)|

* Extracellular signal-regulated
* MAPK1
* MAPK3
* MAPK4
* MAPK6
* MAPK7
* MAPK12
* MAPK15
* C-Jun N-terminal
* MAPK8
* MAPK9
* MAPK10
* P38 mitogen-activated protein
* MAPK11
* MAPK13
* MAPK14

MAP3K (EC 2.7.11.25)|

* MAP kinase kinase kinases
* MAP3K1
* MAP3K2
* MAP3K3
* MAP3K4
* MAP3K5
* MAP3K6
* MAP3K7
* MAP3K8
* RAFs
* ARAF
* BRAF
* KSR1
* KSR2
* MLKs
* MAP3K12
* MAP3K13
* MAP3K9
* MAP3K10
* MAP3K11
* MAP3K7
* ZAK
* CDC7
* MAP3K14

Tau-protein kinase (EC 2.7.11.26)|

* TPK1
* TTK
* GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)|

* -

Tropomyosin kinase (EC 2.7.11.28)|

* -

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)|

* -

Receptor protein serine/threonine kinase (EC 2.7.11.30)|

* Bone morphogenetic protein receptors
* BMPR1
* BMPR1A
* BMPR1B
* BMPR2
* ACVR1
* ACVR1B
* ACVR1C
* ACVR2A
* ACVR2B
* ACVRL1
* Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

| MAP2K|

* MAP2K1
* MAP2K2
* MAP2K3
* MAP2K4
* MAP2K5
* MAP2K6
* MAP2K7

|

* 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)

Portal:

* Biology

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