Myeloblastin

Myeloblastin
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

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

  1. 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 52692Freely accessible. PMID 1681549.
  2. 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.
  3. 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.
  4. 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

This article is issued from Wikipedia - version of the 5/22/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.