AXL receptor tyrosine kinase

Protein-coding gene in the species Homo sapiens

AXL

| Available structures

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

2C5D, 4RA0

Identifiers
Aliases| AXL, AZF, AZFA, SP3, AZF1, ARK, JTK11, Tyro7, UFO, AXL receptor tyrosine kinase
External IDs| OMIM: 109135; MGI: 1347244; HomoloGene: 7583; GeneCards: AXL; OMA:AXL - orthologs
| Gene location (Human)

Chr.| Chromosome 19 (human)[1]

Band| 19q13.2| Start| 41,219,223 bp[1]
End| 41,261,766 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 7 (mouse)[2]

Band| 7 A3|7 14.02 cM| Start| 25,456,698 bp[2]
End| 25,488,130 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* synovial joint

* saphenous vein

* stromal cell of endometrium

* cartilage tissue

* synovial membrane

* urethra

* pericardium

* decidua

* popliteal artery

* tibial arteries

| Top expressed in

* Gonadal ridge

* ascending aorta

* aortic valve

* umbilical cord

* ankle joint

* lip

* ankle

* efferent ductule

* stroma of bone marrow

* uterus

More reference expression data
BioGPS| |

More reference expression data
| Gene ontology

Molecular function|

* nucleotide binding
* protein kinase activity
* transferase activity
* virus receptor activity
* kinase activity
* protein heterodimerization activity
* ATP binding
* phosphatidylserine binding
* protein binding
* transmembrane receptor protein tyrosine kinase activity
* phosphatidylinositol 3-kinase binding
* myosin heavy chain binding
* protein tyrosine kinase activity
* Wnt-protein binding

Cellular component|

* extracellular exosome
* integral component of membrane
* host cell surface
* integral component of plasma membrane
* cell surface
* membrane
* intracellular anatomical structure
* plasma membrane
* extracellular space
* receptor complex

Biological process|

* protein kinase B signaling
* positive regulation of natural killer cell differentiation
* apoptotic cell clearance
* negative regulation of lymphocyte activation
* spermatogenesis
* negative regulation of apoptotic process
* signal transduction
* natural killer cell differentiation
* negative regulation of interferon-gamma production
* cellular response to lipopolysaccharide
* secretion by cell
* vascular endothelial growth factor receptor signaling pathway
* substrate adhesion-dependent cell spreading
* erythrocyte homeostasis
* negative regulation of tumor necrosis factor production
* positive regulation of protein kinase B signaling
* viral process
* positive regulation of cytokine-mediated signaling pathway
* cellular response to interferon-alpha
* forebrain cell migration
* viral entry into host cell
* negative regulation of dendritic cell apoptotic process
* protein phosphorylation
* cellular response to extracellular stimulus
* enzyme linked receptor protein signaling pathway
* positive regulation of pinocytosis
* negative regulation of neuron apoptotic process
* vagina development
* ovulation cycle
* innate immune response
* blood vessel remodeling
* cell maturation
* dendritic cell differentiation
* platelet activation
* cell differentiation
* immune system process
* inflammatory response
* neuron migration
* phosphorylation
* cellular response to hydrogen peroxide
* animal organ regeneration
* phagocytosis
* peptidyl-tyrosine phosphorylation
* negative regulation of cytokine production
* neutrophil clearance
* transmembrane receptor protein tyrosine kinase signaling pathway
* nervous system development
* Wnt signaling pathway
* cell migration

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

558

26362

Ensembl| |

ENSG00000167601

ENSMUSG00000002602

UniProt| |

P30530

Q00993

RefSeq (mRNA)| |

NM_001278599
NM_001699
NM_021913

NM_001190974
NM_001190975
NM_009465

RefSeq (protein)| |

NP_001265528
NP_001690
NP_068713

NP_001177903
NP_001177904
NP_033491

Location (UCSC)| Chr 19: 41.22 – 41.26 Mb| Chr 7: 25.46 – 25.49 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

Tyrosine-protein kinase receptor UFO is a protein that in human is encoded by the AXL gene.[5][6] The gene was initially designated as UFO, in allusion to the unidentified function of this protein.[7] However, in the years since its discovery, research into AXL's expression profile and mechanism has made it an increasingly attractive target, especially for cancer therapeutics. In recent years, AXL has emerged as a key facilitator of immune escape and drug-resistance by cancer cells, leading to aggressive and metastatic cancers.[8]

AXL is a cell surface receptor tyrosine kinase, part of the TAM family of kinases including TYRO3 and MERTK.[9]

## Gene

[edit]

The Axl gene is evolutionarily conserved between vertebrate species.

Human AXL is in close vicinity to the BCL3 oncogene, which is at 19q13.1-q13.2.[6] This gene has two different alternatively spliced transcript variants.[6]

## Structure

[edit]

The protein encoded by this gene is a member of the receptor tyrosine kinase subfamily. Although it is similar to other receptor tyrosine kinases, the Axl protein represents a unique structure of the extracellular region that juxtaposes IgL and FNIII repeats.[6]

The AXL protein is characterized by an extracellular structure consisting of two fibronectin type 3-like repeats and two immunoglobulin-like repeats along with its intracellular tyrosine kinase domain.

## Function

[edit]

The AXL receptor transduces signals from the extracellular matrix into the cytoplasm by binding growth factors like vitamin K-dependant protein growth-arrest-specific gene 6 (GAS6). It is involved in the stimulation of cell proliferation, migration, differentiation and survival. Activation of Axl leads to autophosphorylation of its intracellular domain. Proteolytic cleavage of the AXL extracellular domain by the metalloproteinases ADAM10 and ADAM17 can downregulate this signalling activity.[10]

Signalling pathways activated downstream of AXL include PI3K-AKT-mTOR, MEKERK, NF-κB, and JAK/STAT.[11]

This receptor can also mediate cell aggregation by homophilic binding.[6]

AXL protein is expressed in normal tissues, particularly in bone marrow stroma and myeloid cells, and in tumour cells and tumour vasculature.[12][13] In cancer, AXL is expressed on the tumor cells as well as adjacent immune cells including dendritic cells, macrophages, and NK cells.

Axl is an inhibitor of the innate immune response. The function of activated AXL in normal tissues includes the efficient clearance of apoptotic material and the dampening of TLR-dependent inflammatory responses and natural killer cell activity.[14]

Axl expression on dendritic cells has been shown to limit their maturation and functions by limiting cholesterol mobilization for the assembly of lipid nanodomains at the cell surface.[15]

AXL is a putative driver of diverse cellular processes that are critical for the development, growth, and spread of tumours, including proliferation, invasiveness and migration, epithelial-to-mesenchymal transition, stemness, angiogenesis, and immune modulation.[11] AXL has been implicated as a cancer driver and correlated with poor survival in numerous aggressive tumors including triple-negative breast cancer (TNBC), acute myeloid leukemia (AML), non-small-cell lung cancer (NSCLC), pancreatic cancer and ovarian cancer, among others.[16]

## Clinical significance

[edit]

Axl was first isolated in 1988 and identified as an oncogene in a screen for transforming genes in patients with a chronic myelogenous leukemia\- that progressed to 'blast crisis'.[17] Since then, increased AXL expression has been associated with numerous cancers including lung cancer, breast cancer, pancreatic cancer, ovarian cancer, colon cancer and melanoma among others, and shown to have a strong correlation with poor survival outcomes.[13]

AXL has been shown to be a key driver of drug-resistance to targeted therapies, immuno therapies and chemotherapy in various animal models. Based on current knowledge of AXL's role in therapy resistance, future studies will help to determine whether AXL has a translational application as a biomarker for predicting therapeutic response to established drugs.

Recently, AXL has been implicated in chronic fibrotic diseases in several organs, including the liver.[18]

AXL also play an important role in Zika virus and SARS-CoV-2 infection, allowing for entry of the virus into host cells.[19] [20] This phenomenon is known to rely on phosphatidylserine incorporated in the viral envelope during egress, which then binds to AXL via the adapter GAS6. AXL mediates internalization into the endosome from which these viruses escape and initiate replication.

## As a drug target

[edit]

Studies have shown that AXL knockdown leads to downregulation of transcription factors required for EMT, including Slug, Twist, and Zeb1, and to increased expression of E-cadherin.[21]

### Cancer

[edit]

Several drugs classified as "AXL inhibitors" have entered clinical trials; however, many target multiple kinase receptors in addition to AXL. The most advanced AXL selective inhibitor is bemcentinib (BGB324 or R428), an oral small molecule currently in multiple Phase II clinical trials for NSCLC, TNBC, AML and melanoma. Bemcentinib is being pursued as monotherapy and as combination therapy with existing and emerging targeted therapies, immunotherapies and chemotherapy.

A monoclonal antibody targeting AXL (YW327.6S2) and an AXL decoy receptor (GL2I.T) are currently in preclinical development. Additionally, an oral AXL inhibitor (TP-0903) is expected to enter Phase 1 clinical trial in November 2016 (in advanced solid tumours: NCT02729298).

Astellas Pharma is currently testing gilteritinib (ASP2215), a dual FLT3-AXL tyrosine kinase inhibitor in acute myeloid leukemia (AML). In 2017, gilteritinib gained FDA orphan drug status for AML.[22]

These approved drugs and ongoing and pending clinical trials highlight the potentially wide-ranging safety and efficacy of AXL inhibition.[11]

## Interactions

[edit]

AXL receptor tyrosine kinase has been shown to interact with TENC1.[23] Also, it interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1, and TNS2.[24]

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167601 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002602 – 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. ^ O'Bryan JP, Frye RA, Cogswell PC, Neubauer A, Kitch B, Prokop C, et al. (October 1991). "axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase". Molecular and Cellular Biology. 11 (10): 5016–5031\. doi:10.1128/mcb.11.10.5016. PMC 361494. PMID 1656220.
6. ^ a b c d e "Entrez Gene: AXL AXL receptor tyrosine kinase".
7. ^ Janssen JW, Schulz AS, Steenvoorden AC, Schmidberger M, Strehl S, Ambros PF, et al. (November 1991). "A novel putative tyrosine kinase receptor with oncogenic potential". Oncogene. 6 (11): 2113–2120\. PMID 1834974.
8. ^ Davidsen KT, Haaland GS, Lie MK, Lorens JB, Engelsen AS (2017). "The Role of Axl Receptor Tyrosine Kinase in Tumor Cell Plasticity and Therapy Resistance". In Akslen L, Watnick R (eds.). Biomarkers of the Tumor Microenvironment. Cham: Springer. pp. 351–376\. ISBN 978-3-319-39147-2.
9. ^ Miao YR, Rankin EB, Giaccia AJ (March 2024). "Therapeutic targeting of the functionally elusive TAM receptor family". Nature Reviews. Drug Discovery. 23 (3): 201–217\. doi:10.1038/s41573-023-00846-8. PMC 11335090. PMID 38092952.
10. ^ Miller MA, Oudin MJ, Sullivan RJ, Wang SJ, Meyer AS, Im H, et al. (April 2016). "Reduced Proteolytic Shedding of Receptor Tyrosine Kinases Is a Post-Translational Mechanism of Kinase Inhibitor Resistance". Cancer Discovery. 6 (4): 382–399\. doi:10.1158/2159-8290.CD-15-0933. PMC 5087317. PMID 26984351.
11. ^ a b c Gay CM, Balaji K, Byers LA (February 2017). "Giving AXL the axe: targeting AXL in human malignancy". British Journal of Cancer. 116 (4): 415–423\. doi:10.1038/bjc.2016.428. PMC 5318970. PMID 28072762.
12. ^ Neubauer A, Fiebeler A, Graham DK, O'Bryan JP, Schmidt CA, Barckow P, et al. (September 1994). "Expression of axl, a transforming receptor tyrosine kinase, in normal and malignant hematopoiesis". Blood. 84 (6): 1931–1941\. doi:10.1182/blood.V84.6.1931.1931. PMID 7521695.
13. ^ a b Shieh YS, Lai CY, Kao YR, Shiah SG, Chu YW, Lee HS, et al. (December 2005). "Expression of axl in lung adenocarcinoma and correlation with tumor progression". Neoplasia. 7 (12): 1058–1064\. doi:10.1593/neo.05640. PMC 1501169. PMID 16354588.
14. ^ Rothlin CV, Ghosh S, Zuniga EI, Oldstone MB, Lemke G (December 2007). "TAM receptors are pleiotropic inhibitors of the innate immune response". Cell. 131 (6): 1124–1136\. doi:10.1016/j.cell.2007.10.034. PMID 18083102.
15. ^ Belabed M, Park MD, Blouin CM, Balan S, Moon CY, Freed G, et al. (February 2025). "Cholesterol mobilization regulates dendritic cell maturation and the immunogenic response to cancer". Nature Immunology. 26 (2): 188–199\. doi:10.1038/s41590-024-02065-8. PMID 39838105.
16. ^ Vajkoczy P, Knyazev P, Kunkel A, Capelle HH, Behrndt S, von Tengg-Kobligk H, et al. (April 2006). "Dominant-negative inhibition of the Axl receptor tyrosine kinase suppresses brain tumor cell growth and invasion and prolongs survival". Proceedings of the National Academy of Sciences of the United States of America. 103 (15): 5799–5804\. Bibcode:2006PNAS..103.5799V. doi:10.1073/pnas.0510923103. PMC 1458653. PMID 16585512.
17. ^ Liu E, Hjelle B, Bishop JM (March 1988). "Transforming genes in chronic myelogenous leukemia". Proceedings of the National Academy of Sciences of the United States of America. 85 (6): 1952–1956\. Bibcode:1988PNAS...85.1952L. doi:10.1073/pnas.85.6.1952. PMC 279899. PMID 3279421.
18. ^ Bárcena C, Stefanovic M, Tutusaus A, Joannas L, Menéndez A, García-Ruiz C, et al. (September 2015). "Gas6/Axl pathway is activated in chronic liver disease and its targeting reduces fibrosis via hepatic stellate cell inactivation". Journal of Hepatology. 63 (3): 670–678\. doi:10.1016/j.jhep.2015.04.013. PMC 4543529. PMID 25908269.
19. ^ Nowakowski TJ, Pollen AA, Di Lullo E, Sandoval-Espinosa C, Bershteyn M, Kriegstein AR (May 2016). "Expression Analysis Highlights AXL as a Candidate Zika Virus Entry Receptor in Neural Stem Cells". Cell Stem Cell. 18 (5): 591–596\. doi:10.1016/j.stem.2016.03.012. PMC 4860115. PMID 27038591.
20. ^ Bohan D, Van Ert H, Ruggio N, Rogers KJ, Badreddine M, Aguilar Briseño JA, et al. (November 2021). "Phosphatidylserine receptors enhance SARS-CoV-2 infection". PLoS Pathogens. 17 (11): e1009743. doi:10.1371/journal.ppat.1009743. PMC 8641883. PMID 34797899.
21. ^ Asiedu MK, Beauchamp-Perez FD, Ingle JN, Behrens MD, Radisky DC, Knutson KL (March 2014). "AXL induces epithelial-to-mesenchymal transition and regulates the function of breast cancer stem cells". Oncogene. 33 (10): 1316–1324\. doi:10.1038/onc.2013.57. PMC 3994701. PMID 23474758.
22. ^ Nam J (July 20, 2017). "Gilteritinib Granted Orphan Drug Status for Acute Myeloid Leukemia". Cancer Therapy Advisor. Haymarket Media Inc.
23. ^ Hafizi S, Alindri F, Karlsson R, Dahlbäck B (December 2002). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochemical and Biophysical Research Communications. 299 (5): 793–800\. doi:10.1016/S0006-291X(02)02718-3. PMID 12470648.
24. ^ Hafizi S, Alindri F, Karlsson R, Dahlbäck B (December 2002). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochemical and Biophysical Research Communications. 299 (5): 793–800\. doi:10.1016/S0006-291X(02)02718-3. PMID 12470648.

## Further reading

[edit]

* Neubauer A, Burchert A, Maiwald C, Gruss HJ, Serke S, Huhn D, et al. (March 1997). "Recent progress on the role of Axl, a receptor tyrosine kinase, in malignant transformation of myeloid leukemias". Leukemia & Lymphoma. 25 (1–2): 91–96\. doi:10.3109/10428199709042499. PMID 9130617.1–2&rft.pages=91-96&rft.date=1997-03&rft_id=info:doi/10.3109/10428199709042499&rft_id=info:pmid/9130617&rft.aulast=Neubauer&rft.aufirst=A&rft.au=Burchert,+A&rft.au=Maiwald,+C&rft.au=Gruss,+HJ&rft.au=Serke,+S&rft.au=Huhn,+D&rft.au=Wittig,+B&rft.au=Liu,+E&rfr_id=info:sid/en.wikipedia.org:AXL+receptor+tyrosine+kinase" class="Z3988">
* Bergsagel PL, Victor-Kobrin C, Timblin CR, Trepel J, Kuehl WM (January 1992). "A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed on plasma cells". Journal of Immunology. 148 (2): 590–596\. doi:10.4049/jimmunol.148.2.590. PMID 1729376.
* Partanen J, Mäkelä TP, Alitalo R, Lehväslaiho H, Alitalo K (November 1990). "Putative tyrosine kinases expressed in K-562 human leukemia cells". Proceedings of the National Academy of Sciences of the United States of America. 87 (22): 8913–8917\. Bibcode:1990PNAS...87.8913P. doi:10.1073/pnas.87.22.8913. PMC 55070. PMID 2247464.
* O'Bryan JP, Fridell YW, Koski R, Varnum B, Liu ET (January 1995). "The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage". The Journal of Biological Chemistry. 270 (2): 551–557\. doi:10.1074/jbc.270.2.551. PMID 7822279.
* Lee ST, Strunk KM, Spritz RA (December 1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene. 8 (12): 3403–3410\. PMID 8247543.
* Schulz AS, Schleithoff L, Faust M, Bartram CR, Janssen JW (February 1993). "The genomic structure of the human UFO receptor". Oncogene. 8 (2): 509–513\. PMID 8381225.
* O'Bryan JP, Songyang Z, Cantley L, Der CJ, Pawson T (April 1996). "A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain". Proceedings of the National Academy of Sciences of the United States of America. 93 (7): 2729–2734\. Bibcode:1996PNAS...93.2729O. doi:10.1073/pnas.93.7.2729. PMC 39699. PMID 8610109.
* Mark MR, Chen J, Hammonds RG, Sadick M, Godowsk PJ (April 1996). "Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl". The Journal of Biological Chemistry. 271 (16): 9785–9789\. doi:10.1074/jbc.271.16.9785. PMID 8621659.
* Braunger J, Schleithoff L, Schulz AS, Kessler H, Lammers R, Ullrich A, et al. (June 1997). "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site". Oncogene. 14 (22): 2619–2631\. doi:10.1038/sj.onc.1201123. PMID 9178760.
* Tanaka K, Nagayama Y, Nakano T, Takamura N, Namba H, Fukada S, et al. (March 1998). "Expression profile of receptor-type protein tyrosine kinase genes in the human thyroid". Endocrinology. 139 (3): 852–858\. doi:10.1210/en.139.3.852. PMID 9492013.
* Yanagita M, Arai H, Ishii K, Nakano T, Ohashi K, Mizuno K, et al. (April 2001). "Gas6 regulates mesangial cell proliferation through Axl in experimental glomerulonephritis". The American Journal of Pathology. 158 (4): 1423–1432\. doi:10.1016/S0002-9440(10)64093-X. PMC 1891897. PMID 11290560.
* Sun WS, Misao R, Iwagaki S, Fujimoto J, Tamaya T (June 2002). "Coexpression of growth arrest-specific gene 6 and receptor tyrosine kinases, Axl and Sky, in human uterine endometrium and ovarian endometriosis". Molecular Human Reproduction. 8 (6): 552–558\. doi:10.1093/molehr/8.6.552. PMID 12029073.
* D'Arcangelo D, Gaetano C, Capogrossi MC (October 2002). "Acidification prevents endothelial cell apoptosis by Axl activation". Circulation Research. 91 (7): e4-12. doi:10.1161/01.RES.0000036753.50601.E9. PMID 12364394.
* Ito M, Nakashima M, Nakayama T, Ohtsuru A, Nagayama Y, Takamura N, et al. (November 2002). "Expression of receptor-type tyrosine kinase, Axl, and its ligand, Gas6, in pediatric thyroid carcinomas around chernobyl". Thyroid. 12 (11): 971–975\. doi:10.1089/105072502320908303. PMID 12490074.

## External links

[edit]

* Human AXL genome location and AXL gene details page in the UCSC Genome Browser.
* Overview of all the structural information available in the PDB for UniProt: P30530 (Tyrosine-protein kinase receptor UFO) at the PDBe-KB.

* v
* t
* e

PDB gallery

* 2c5d: STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX

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* e

Protein kinases: tyrosine kinases (EC 2.7.10)

Receptor tyrosine kinases (EC 2.7.10.1)

| Growth factor receptors|

| EGF receptor family|

* EGFR
* ERBB2
* ERBB3
* ERBB4

|

Insulin receptor family|

* IGF1R
* INSR
* INSRR

PDGF receptor family|

* CSF1R
* FLT3
* KIT
* PDGFR (PDGFRA
* PDGFRB)

FGF receptor family|

* FGFR1
* FGFR2
* FGFR3
* FGFR4

VEGF receptors family|

* VEGFR1
* VEGFR2
* VEGFR3

HGF receptor family|

* MET
* RON

Trk receptor family|

* NTRK1
* NTRK2
* NTRK3

EPH receptor family|

* EPHA1
* EPHA2
* EPHA3
* EPHA4
* EPHA5
* EPHA6
* EPHA7
* EPHA8
* EPHB1
* EPHB2
* EPHB3
* EPHB4
* EPHB5
* EPHB6
* EPHX

LTK receptor family|

* LTK
* ALK

TIE receptor family|

* TIE
* TEK

ROR receptor family|

* ROR1
* ROR2

DDR receptor family|

* DDR1
* DDR2

PTK7 receptor family|

* PTK7

RYK receptor family|

* RYK

MuSK receptor family|

* MUSK

ROS receptor family|

* ROS1

AATYK receptor family|

* AATYK
* AATYK2

AXL receptor family|

* AXL
* MER
* TYRO3

RET receptor family|

* RET

uncategorised|

* STYK1

Non-receptor tyrosine kinases (EC 2.7.10.2)

| ABL family|

* ABL1
* ARG

|

ACK family|

* ACK1
* TNK1

CSK family|

* CSK
* MATK

FAK family|

* FAK
* PYK2

FES family|

* FES
* FER

FRK family|

* FRK
* BRK
* SRMS

JAK family|

* JAK1
* JAK2
* JAK3
* TYK2

SRC-A family|

* SRC
* FGR
* FYN
* YES1

SRC-B family|

* BLK
* HCK
* LCK
* LYN

TEC family|

* TEC
* BMX
* BTK
* ITK
* TXK

SYK family|

* SYK
* ZAP70

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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)

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