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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]

References

^ Martin KR, Witko-Sarsat V (September 2017). "Proteinase 3: the odd one out that became an autoantigen". Journal of Leukocyte Biology. 102 (3): 689–698. doi:10.1189/jlb.3MR0217-069R. PMID 28546501.
^ Brubaker MJ, Groutas WC, Hoidal JR, Rao NV (November 1992). "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochemical and Biophysical Research Communications. 188 (3): 1318–24. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.
^ Kam CM, Kerrigan JE, Dolman KM, Goldschmeding R, Von dem Borne AE, Powers JC (February 1992). "Substrate and inhibitor studies on proteinase 3". FEBS Letters. 297 (1–2): 119–23. doi:10.1016/0014-5793(92)80340-m. PMID 1551417.
^ Bories D, Raynal MC, Solomon DH, Darzynkiewicz Z, Cayre YE (December 1989). "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell. 59 (6): 959–68. doi:10.1016/0092-8674(89)90752-6. PMID 2598267.

External links

Myeloblastin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[Martin2017-1] Martin KR, Witko-Sarsat V (September 2017). "Proteinase 3: the odd one out that became an autoantigen". Journal of Leukocyte Biology. 102 (3): 689–698. doi:10.1189/jlb.3MR0217-069R. PMID 28546501.

[2] Brubaker MJ, Groutas WC, Hoidal JR, Rao NV (November 1992). "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochemical and Biophysical Research Communications. 188 (3): 1318–24. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.

[3] Kam CM, Kerrigan JE, Dolman KM, Goldschmeding R, Von dem Borne AE, Powers JC (February 1992). "Substrate and inhibitor studies on proteinase 3". FEBS Letters. 297 (1–2): 119–23. doi:10.1016/0014-5793(92)80340-m. PMID 1551417.

[pmid2598267-4] Bories D, Raynal MC, Solomon DH, Darzynkiewicz Z, Cayre YE (December 1989). "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell. 59 (6): 959–68. doi:10.1016/0092-8674(89)90752-6. PMID 2598267.

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Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

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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References

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