Biology:Myeloblastin
From HandWiki
| 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] 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. Downregulation of myeloblastin in promyelocytic leukemia cells was shown to induce their growth arrest and differentiation.[4]
See also
References
- ↑ "Proteinase 3: the odd one out that became an autoantigen". Journal of Leukocyte Biology 102 (3): 689–698. September 2017. doi:10.1189/jlb.3MR0217-069R. PMID 28546501.
- ↑ "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochemical and Biophysical Research Communications 188 (3): 1318–24. November 1992. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.
- ↑ "Substrate and inhibitor studies on proteinase 3". FEBS Letters 297 (1-2): 119–23. February 1992. doi:10.1016/0014-5793(92)80340-m. PMID 1551417.
- ↑ "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell 59 (6): 959–68. December 1989. doi:10.1016/0092-8674(89)90752-6. PMID 2598267.
External links
- Myeloblastin at the US National Library of Medicine Medical Subject Headings (MeSH)
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