Myeloblastin
Myeloblastin | |||||||||
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Identifiers | |||||||||
EC number | 3.4.21.76 | ||||||||
CAS number | 128028-50-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Myeloblastin (EC 3.4.21.76, leukocyte proteinase 3, leukocyte proteinase 4, Wegener's granulomatosis autoantigen, proteinase PR-3, proteinase-3, PMNL proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala- > -Val-
This enzyme is present in polymorphonuclear leukocyte granules.
References
- ↑ Labbaye, C.; Musette, P.; Cayre, Y.E. (1991). "Wegener autoantigen and myeloblastin are encoded by a single mRNA". Proc. Natl. Acad. Sci. USA. 88: 9253–9256. doi:10.1073/pnas.88.20.9253. PMC 52692. PMID 1681549.
- ↑ Rao, N.V.; Wehner, N.G.; Marshall, B.C.; Gray, W.R.; Gray, B.H.; Hoidal, J.R. (1991). "Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties". J. Biol. Chem. 266 (15): 9540–9548. PMID 2033050.
- ↑ Brubaker, M.J.; Groutas, W.C.; Hoidal, J.R.; Rao, N.V. (1992). "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochem. Biophys. Res. Commun. 188 (3): 1318–1324. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.
- ↑ Kam, C.-M.; Kerrigan, J.E.; Dolman, K.M.; Goldschmeding, R.; von dem Borne, A.E.G.K.; Powers, J.C. (1992). "Substrate and inhibitor studies on proteinase 3". FEBS Lett. 297 (1-2): 119–123. doi:10.1016/0014-5793(92)80340-m. PMID 1551417.
See also
External links
- Myeloblastin at the US National Library of Medicine Medical Subject Headings (MeSH)
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