METAP2

METAP2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1B59, 1B6A, 1BN5, 1BOA, 1KQ0, 1KQ9, 1QZY, 1R58, 1R5G, 1R5H, 1YW7, 1YW8, 1YW9, 2ADU, 2EA2, 2EA4, 2GA2, 2OAZ, 5CLS, 5D6E, 5D6F, 5JFR, 5JHU, 5JI6
Identifiers
Aliases	METAP2, MAP2, MNPEP, p67, p67eIF2, methionyl aminopeptidase 2
External IDs	OMIM: 601870; MGI: 1929701; HomoloGene: 4981; GeneCards: METAP2; OMA:METAP2 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	95,515,839 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	93,732,955 bp
RNA expression pattern
	Top expressed in
	sural nerve; ; seminal vesicula; ; Achilles tendon; ; tendon of biceps brachii; ; trabecular bone; ; oral cavity; ; secondary oocyte; ; ganglionic eminence; ; endometrium; ; epithelium of colon;
	Top expressed in
	neural layer of retina; ; tail of embryo; ; genital tubercle; ; muscle of thigh; ; yolk sac; ; morula; ; ventricular zone; ; embryo; ; spermatid; ; spermatocyte;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	peptidase activity; metalloexopeptidase activity; hydrolase activity; metal ion binding; aminopeptidase activity; RNA binding; metalloaminopeptidase activity;
Cellular component	cytoplasm; plasma membrane; cytosol;
Biological process	peptidyl-methionine modification; protein processing; N-terminal protein amino acid modification; proteolysis; regulation of rhodopsin mediated signaling pathway; protein initiator methionine removal;
	Sources:Amigo / QuickGO
Orthologs
	10988
	56307
	ENSG00000111142
	ENSMUSG00000036112
	P50579
	O08663
	NM_006838; NM_001317182; NM_001317183; NM_001330246
	NM_019648
	NP_001304111; NP_001304112; NP_001317175; NP_006829
	NP_062622
	Wikidata
View/Edit Human	View/Edit Mouse

Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.^[5]^[6]

Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins.^[7]^[8]^[9]

peptide-methionine $\rightleftharpoons$ peptide + methionine

MetAP2 is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation.^[7] Furthermore, MetAP2 is of particular interest because the enzyme plays a key role in angiogenesis, the growth of new blood vessels, which is necessary for the progression of diseases including solid tumor cancers and rheumatoid arthritis.^[10] MetAP2 is also the target of two groups of anti-angiogenic natural products, ovalicin and fumagillin, and their analogs such as beloranib.^[11]^[12]^[13]^[14]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000111142 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036112 – 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.
^ Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, et al. (September 1995). "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes". Proc Natl Acad Sci U S A. 92 (17): 7714–8. Bibcode:1995PNAS...92.7714A. doi:10.1073/pnas.92.17.7714. PMC 41216. PMID 7644482.
^ Li X, Chang YH (November 1996). "Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase". Biochem Biophys Res Commun. 227 (1): 152–9. doi:10.1006/bbrc.1996.1482. PMID 8858118.
^ ^a ^b Bennett B, Holz RC (1997). "EPR Studies on the Mono- and Dicobalt(II)-Substituted Forms of the Aminopeptidase from Aeromonas proteolytica. Insight into the Catalytic Mechanism of Dinuclear Hydrolases". J. Am. Chem. Soc. 119 (8): 1923–1933. doi:10.1021/ja963021v.
^ Johansson FB, Bond AD, Nielsen UG, Moubaraki B, Murray KS, Berry KJ, et al. (June 2008). "Dicobalt II-II, II-III, and III-III complexes as spectroscopic models for dicobalt enzyme active sites". Inorg Chem. 47 (12): 5079–92. doi:10.1021/ic7020534. PMID 18494467.
^ Larrabee JA, Leung CH, Moore RL, Thamrong-nawasawat T, Wessler BS (October 2004). "Magnetic circular dichroism and cobalt(II) binding equilibrium studies of Escherichia coli methionyl aminopeptidase". J. Am. Chem. Soc. 126 (39): 12316–24. doi:10.1021/ja0485006. PMID 15453765.
^ Folkman J (January 1995). "Angiogenesis in cancer, vascular, rheumatoid and other disease". Nat. Med. 1 (1): 27–31. doi:10.1038/nm0195-27. PMID 7584949. S2CID 5924813.
^ Taunton J (July 1997). "How to starve a tumor". Chem. Biol. 4 (7): 493–6. doi:10.1016/S1074-5521(97)90320-3. PMID 9263636.
^ Sin N, Meng L, Wang MQ, Wen JJ, Bornmann WG, Crews CM (June 1997). "The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6099–103. Bibcode:1997PNAS...94.6099S. doi:10.1073/pnas.94.12.6099. PMC 21008. PMID 9177176.
^ Griffith EC, Su Z, Turk BE, Chen S, Chang YH, Wu Z, et al. (June 1997). "Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin". Chem. Biol. 4 (6): 461–71. doi:10.1016/S1074-5521(97)90198-8. PMID 9224570.
^ Lowther WT, McMillen DA, Orville AM, Matthews BW (October 1998). "The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12153–7. Bibcode:1998PNAS...9512153L. doi:10.1073/pnas.95.21.12153. PMC 22800. PMID 9770455.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000111142 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000036112 – 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.

[pmid7644482-5] Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, et al. (September 1995). "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes". Proc Natl Acad Sci U S A. 92 (17): 7714–8. Bibcode:1995PNAS...92.7714A. doi:10.1073/pnas.92.17.7714. PMC 41216. PMID 7644482.

[pmid8858118-6] Li X, Chang YH (November 1996). "Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase". Biochem Biophys Res Commun. 227 (1): 152–9. doi:10.1006/bbrc.1996.1482. PMID 8858118.

[isbnunkn1-7] Bennett B, Holz RC (1997). "EPR Studies on the Mono- and Dicobalt(II)-Substituted Forms of the Aminopeptidase from Aeromonas proteolytica. Insight into the Catalytic Mechanism of Dinuclear Hydrolases". J. Am. Chem. Soc. 119 (8): 1923–1933. doi:10.1021/ja963021v.

[isbnunkn2-8] Johansson FB, Bond AD, Nielsen UG, Moubaraki B, Murray KS, Berry KJ, et al. (June 2008). "Dicobalt II-II, II-III, and III-III complexes as spectroscopic models for dicobalt enzyme active sites". Inorg Chem. 47 (12): 5079–92. doi:10.1021/ic7020534. PMID 18494467.

[isbnunkn3-9] Larrabee JA, Leung CH, Moore RL, Thamrong-nawasawat T, Wessler BS (October 2004). "Magnetic circular dichroism and cobalt(II) binding equilibrium studies of Escherichia coli methionyl aminopeptidase". J. Am. Chem. Soc. 126 (39): 12316–24. doi:10.1021/ja0485006. PMID 15453765.

[isbnunkn4-10] Folkman J (January 1995). "Angiogenesis in cancer, vascular, rheumatoid and other disease". Nat. Med. 1 (1): 27–31. doi:10.1038/nm0195-27. PMID 7584949. S2CID 5924813.

[Taunton-11] Taunton J (July 1997). "How to starve a tumor". Chem. Biol. 4 (7): 493–6. doi:10.1016/S1074-5521(97)90320-3. PMID 9263636.

[isbnunkn7-12] Sin N, Meng L, Wang MQ, Wen JJ, Bornmann WG, Crews CM (June 1997). "The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6099–103. Bibcode:1997PNAS...94.6099S. doi:10.1073/pnas.94.12.6099. PMC 21008. PMID 9177176.

[isbnunkn8-13] Griffith EC, Su Z, Turk BE, Chen S, Chang YH, Wu Z, et al. (June 1997). "Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin". Chem. Biol. 4 (6): 461–71. doi:10.1016/S1074-5521(97)90198-8. PMID 9224570.

[isbnunkn9-14] Lowther WT, McMillen DA, Orville AM, Matthews BW (October 1998). "The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12153–7. Bibcode:1998PNAS...9512153L. doi:10.1073/pnas.95.21.12153. PMC 22800. PMID 9770455.

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