Macrophage elastase: Difference between revisions

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Macrophage elastase
Macrophage elastase
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EC no.	3.4.24.65
CAS no.	2594837
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Macrophage elastase (EC 3.4.24.65, metalloelastase, human macrophage metalloelastase (HME), MMP-12) is an enzyme.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala¹⁴-Leu- and -Tyr¹⁶-Leu- in the B chain of insulin

This enzyme belongs to the peptidase family M10.

References

^ Banda MJ, Werb Z (February 1981). "Mouse macrophage elastase. Purification and characterization as a metalloproteinase". The Biochemical Journal. 193 (2): 589–605. PMID 7030312.
^ Kettner C, Shaw E, White R, Janoff A (May 1981). "The specificity of macrophage elastase on the insulin B-chain". The Biochemical Journal. 195 (2): 369–72. PMID 7032505.
^ Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ (March 1992). "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase". The Journal of Biological Chemistry. 267 (7): 4664–71. PMID 1537850.
^ Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". The Journal of Biological Chemistry. 268 (32): 23824–9. PMID 8226919.

External links

Macrophage+elastase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Banda MJ, Werb Z (February 1981). "Mouse macrophage elastase. Purification and characterization as a metalloproteinase". The Biochemical Journal. 193 (2): 589–605. PMID 7030312.

[2] Kettner C, Shaw E, White R, Janoff A (May 1981). "The specificity of macrophage elastase on the insulin B-chain". The Biochemical Journal. 195 (2): 369–72. PMID 7032505.

[3] Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ (March 1992). "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase". The Journal of Biological Chemistry. 267 (7): 4664–71. PMID 1537850.

[4] Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". The Journal of Biological Chemistry. 268 (32): 23824–9. PMID 8226919.

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 {{Infobox enzyme
-| Name = Macrophage elastase
+| Name       = Macrophage elastase
-| EC_number = 3.4.24.65
+| EC_number  = 3.4.24.65
 | CAS_number = 2594837
+| GO_code    =
-| IUBMB_EC_number = 3/4/24/65
-| GO_code =
+| image      =
-| image =
+| width      =
-| width =
+| caption    =
-| caption =
 }}
-'''Macrophage elastase''' ({{EC number|3.4.24.65}}, ''metalloelastase'', ''human macrophage metalloelastase (HME)'') is an [[enzyme]].<ref>{{cite journal | title = Mouse macrophage elastase. Purification and characterization as a metalloproteinase |author = Banda, M.J. and Werb, Z. |journal = Biochem. J. |date = 1981 |volume = 193 |pages = 589-605 |pmid = 7030312}}</ref><ref>{{cite journal | title = The specificity of macrophage elastase on the insulin B-chain |author = Kettner, C., Shaw, E., White, R. and Janoff, A. |journal = Biochem. J. |date = 1981 |volume = 195 |pages = 369-372 |pmid = 7032505}}</ref><ref>{{cite journal | title = Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase |author = Shapiro, S.D., Griffin, G.L., Gilbert, D.J., Jenkins, N.A., Copeland, N.G., Welgus, H.G., Senior, R.M. and Ley, T.J. |journal = J. Biol. Chem. |date = 1992 |volume = 267 |pages = 4664-4671 |pmid = 1537850}}</ref><ref>{{cite journal | title = Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages |author = Shapiro, S.D., Kobayashi, D.K. and Ley, T.J. |journal = J. Biol. Chem. |date = 1993 |volume = 268 |pages = 23824-23829 |pmid = 8226919}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
+'''Macrophage elastase''' ({{EC number|3.4.24.65}}, ''metalloelastase'', ''human macrophage metalloelastase (HME), [[Matrix metallopeptidase 12|MMP-12]]'') is an [[enzyme]].<ref>{{cite journal | vauthors = Banda MJ, Werb Z | title = Mouse macrophage elastase. Purification and characterization as a metalloproteinase | journal = The Biochemical Journal | volume = 193 | issue = 2 | pages = 589–605 | date = February 1981 | pmid = 7030312 }}</ref><ref>{{cite journal | vauthors = Kettner C, Shaw E, White R, Janoff A | title = The specificity of macrophage elastase on the insulin B-chain | journal = The Biochemical Journal | volume = 195 | issue = 2 | pages = 369–72 | date = May 1981 | pmid = 7032505 }}</ref><ref>{{cite journal | vauthors = Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ | title = Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase | journal = The Journal of Biological Chemistry | volume = 267 | issue = 7 | pages = 4664–71 | date = March 1992 | pmid = 1537850 }}</ref><ref>{{cite journal | vauthors = Shapiro SD, Kobayashi DK, Ley TJ | title = Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages | journal = The Journal of Biological Chemistry | volume = 268 | issue = 32 | pages = 23824–9 | date = November 1993 | pmid = 8226919 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
-: [[Hydrolysis]] of soluble and insoluble [[elastin]]]. Specific cleavages are also produced at -Ala<sup>14</sup>-Leu- and -Tyr<sup>16</sup>-Leu- in the B chain of [[insulin]]
+: [[Hydrolysis]] of soluble and insoluble [[elastin]]. Specific cleavages are also produced at -Ala<sup>14</sup>-Leu- and -Tyr<sup>16</sup>-Leu- in the B chain of [[insulin]]
 This enzyme belongs to the peptidase family M10.
-== References ==
-{{reflist}}
 == See also ==
 * [[Matrix metallopeptidase 12]]
+== References ==
+{{reflist}}
 == External links ==
 * {{MeshName|Macrophage+elastase}}
+{{Metalloendopeptidases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
 [[Category:EC 3.4.24]]

v t e Proteases: metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e 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)