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Literature summary for 3.4.21.B7 extracted from

  • Dobo, J.; Schroeder, V.; Jenny, L.; Cervenak, L.; Zavodszky, P.; Gal, P.
    Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation (2014), Mol. Immunol., 61, 69-78.
    View publication on PubMed
Search for more literature for 3.4.21.B7

Inhibitors

Inhibitors Comment Organism Structure
antithrombin the inhibitor is not specific for MASP-1 versus MASP-2 Homo sapiens
lectin pathway C1-inhibitor the inhibitor is not specific for MASP-1 versus MASP-2 Homo sapiens
Schistocerca gregaria protease inhibitor-1 SGMI-1, specific inhibition of MASP-1 isozyme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, enzyme-bound, structure overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
complement component C2 + H2O Homo sapiens a complement substrate, activation ?
-
 ?
fibrinogen + H2O Homo sapiens a noncomplement substrate, activation fibrin + ?
-
 ?
high-molecular weight kininogen + H2O Homo sapiens a noncomplement substrate, activation bradykinin + ?
-
 ?
proform coagulation factor XIII + H2O Homo sapiens a noncomplement substrate, activation mature coagulation factor XIII + ?
-
 ?
proform mannan-binding lectin-associated serine protease 1 + H2O Homo sapiens autocatalytic cleavage, a complement substrate, activation mature mannan-binding lectin-associated serine protease 1 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 2 + H2O Homo sapiens a complement substrate, activation mature mannan-binding lectin-associated serine protease 2 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 3 + H2O Homo sapiens a complement substrate, activation mature mannan-binding lectin-associated serine protease 3 + ?
-
 ?
protease activated receptor 4 + H2O Homo sapiens PAR4, a noncomplement substrate, activation ?
-
 ?
prothrombin + H2O Homo sapiens a noncomplement substrate, activation thrombin + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P48740
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification enzyme MASP-1 performs autoactivation through proteolytic cleavage of its zymogen Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C2 + H2O
-
 Homo sapiens ?
-
 ?
complement component C2 + H2O a complement substrate, activation Homo sapiens ?
-
 ?
complement component C3i + H2O
-
 Homo sapiens ?
-
 ?
fibrinogen + H2O
-
 Homo sapiens fibrin + ?
-
 ?
fibrinogen + H2O a noncomplement substrate, activation Homo sapiens fibrin + ?
-
 ?
high-molecular weight kininogen + H2O a noncomplement substrate, activation Homo sapiens bradykinin + ?
-
 ?
kininogen + H2O
-
 Homo sapiens kinin + ?
-
 ?
additional information the enzyme MASP-1 shows a more relaxed substrate specificity. MASP-1 zymogen is fairly active on small substrates, and itautoactivates rapidly due to its relatively fast zymogen autoacti-vation step Homo sapiens ?
-
 ?
PAR4 + H2O
-
 Homo sapiens ?
-
 ?
proform coagulation factor XIII + H2O
-
 Homo sapiens mature coagulation factor XIII + ?
-
 ?
proform coagulation factor XIII + H2O a noncomplement substrate, activation Homo sapiens mature coagulation factor XIII + ?
-
 ?
proform mannan-binding lectin-associated serine protease 1 + H2O autocatalytic cleavage, a complement substrate, activation Homo sapiens mature mannan-binding lectin-associated serine protease 1 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 1 + H2O autocatalytic cleavage Homo sapiens mature mannan-binding lectin-associated serine protease 1 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 2 + H2O
-
 Homo sapiens mature mannan-binding lectin-associated serine protease 2 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 2 + H2O a complement substrate, activation Homo sapiens mature mannan-binding lectin-associated serine protease 2 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 3 + H2O
-
 Homo sapiens mature mannan-binding lectin-associated serine protease 3 + ?
-
 ?
proform mannan-binding lectin-associated serine protease 3 + H2O a complement substrate, activation Homo sapiens mature mannan-binding lectin-associated serine protease 3 + ?
-
 ?
protease activated receptor 4 + H2O PAR4, a noncomplement substrate, activation Homo sapiens ?
-
 ?
prothrombin + H2O
-
 Homo sapiens thrombin + ?
-
 ?
prothrombin + H2O a noncomplement substrate, activation Homo sapiens thrombin + ?
-
 ?

Subunits

Subunits Comment Organism
dimer enzyme three-dimensional structure analysis, the enzyme monomer domains are CUB1-EGF-CUB2-CCP1-CCP2-SP, standing for C1r/C1s-Uegf-BMP domain 1, epidermal growth factor domain, C1r/C1s-Uegf-BMP domain 2, complement control protein domain 1, complement control protein domain 2, and serine protease domain, overview. the enzyme dimer is formed by binding of monomers via CUB1 and EGF domains Homo sapiens

Synonyms

Synonyms Comment Organism
MASP-1
-
 Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000007
-
 Schistocerca gregaria protease inhibitor-1 pH and temperature not specified in the publication, recombinant enzyme Homo sapiens

General Information

General Information Comment Organism
malfunction increased MASP-1 plasma levels in patients in the suba-cute phase of myocardial infarction, but decreased levels of MASP-1 in patients withacute ischemic stroke Homo sapiens
metabolism both MASP-1 and MASP-2 are essential for lectin pathway activation in normal human serum Homo sapiens
additional information enzyme MASP-1 shows a more relaxed substrate specificity compared to the related complement enzymes, crystal structure analysis, overview. The catalytic triad of zymogen MASP-1 is in an active-like conformation, while the S1 pocket is blocked and the oxyanion hole is distorted, which are typical features of zymogen serine proteases. Upon activation, the new amino-terminus forms a salt-bridge with Asp645 rearranging the surface loopsand allowing the oxyanion hole and the S1 pocket to form. In the structure of zymogen MASP-1 two positive side chains might be able to substitute for the amino-terminus aiding Aspc194to rotateto the active-like position Homo sapiens
physiological function besides playing a crucial role in complement activation, the enzyme also triggers other cascade systems and even cells to mount a more powerful innate immune response, multiple roles of MASP-1 in the initiation of the innate immune response, overview. Enzyme MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling. MASP-1 seems to be a major link between the complementsystem and coagulation. Role of MASP-1 in endothelial cell activation and blood coagulation, and role of the enzyme in cardiovascular diseases, detailed overview Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.4
-
 high-molecular weight kininogen pH and temperature not specified in the publication Homo sapiens
0.45
-
 proform mannan-binding lectin-associated serine protease 1 pH and temperature not specified in the publication Homo sapiens
1.2
-
 proform mannan-binding lectin-associated serine protease 3 pH and temperature not specified in the publication Homo sapiens
6
-
 complement component C3i pH and temperature not specified in the publication Homo sapiens
12
-
 proform mannan-binding lectin-associated serine protease 2 pH and temperature not specified in the publication Homo sapiens
30
-
 Complement component C2 pH and temperature not specified in the publication Homo sapiens
180
-
 protease activated receptor 4 pH and temperature not specified in the publication Homo sapiens