3.4.21.B7: mannan-binding lectin-associated serine protease 1
This is an abbreviated version!
For detailed information about mannan-binding lectin-associated serine protease 1, go to the full flat file.
Word Map on EC 3.4.21.B7
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3.4.21.B7
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masp-3
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silk
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spider
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ficolins
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dragline
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c1s
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ampullate
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spidroins
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convertase
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collagen-like
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clavipes
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collectins
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m-ficolin
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autoactivation
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nephila
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subcomponents
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complement-activating
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c1-inhibitor
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latrodectus
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pattern-recognition
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widow
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fibrinogen-like
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protease-2
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opsonin
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extensibility
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urochord
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c1-inh
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hesperus
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medicine
- 3.4.21.B7
- masp-3
-
silk
- spider
- ficolins
-
dragline
- c1s
-
ampullate
-
spidroins
-
convertase
-
collagen-like
- clavipes
-
collectins
- m-ficolin
-
autoactivation
- nephila
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subcomponents
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complement-activating
- c1-inhibitor
- latrodectus
-
pattern-recognition
- widow
-
fibrinogen-like
-
protease-2
-
opsonin
-
extensibility
-
urochord
-
c1-inh
- hesperus
- medicine
Reaction
endopeptidase activity. It triggers the activation of complement cascade by activating the C4 and C2 components. It activates the C4 component by cleaving the alpha-chain of C4 =
Synonyms
mannan-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease-1, mannose-binding lectin-associated serine protease, MASP-1, MASP1, MBL-associated serine protease, MBL-associated serine protease 1, MBL-associated serine protease-1, MBL-MASP, P100, Ra-reactive factor, RaRF, S01.198
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.B7 - mannan-binding lectin-associated serine protease 1
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REACTION DIAGRAM
benzoyl-L-arginine p-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
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?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
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?
complement component C3 + H2O
complement component C3a + complement component C3b
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activates complement C3
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?
complement-activating component of Ra-reactive factor + H2O
?
cleavage at Arg448-/-Ile449
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?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
a chromogenic thrombin substrate, recombinant human mannose-binding lectin alone fails to cleave the substrate, but cleavage is restored when the recombinant enzyme MASP-1 is added to either MASP-1/-3 KO sera or rhMBL
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?
factor XIII A-chain + H2O
?
catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
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?
fibrinogen beta-chain + H2O
?
cleavage at R44-/-G45 and other sites
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?
high-molecular weight kininogen + H2O
bradykinin + ?
a noncomplement substrate, activation
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?
low-molecular-weight kininogen + H2O
?
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the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
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MASP1 mannan-binding lectin serine protease 1 isoform 1 precursor + H2O
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autodegradation pattern of the MASP-1 CCP1-CCP2-SP fragment. Cleavage occurs at the Arg504-Asp505 bond, which results in the removal of a 6000 Da fragment from the active enzyme. The autolysis of the MASP-1 CCP1-CCP2-SP fragment causes the loss of its enzymatic activity due to the removal of the histidine from the catalytic triad
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N-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
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proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
proform protease activated receptor 4 + H2O
mature protease activated receptor 4 + ?
activation
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?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
complement component C2 + H2O
?
digested by the MASP-1 CCP1-CCP2-SP fragment at a moderate rate
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?
complement component C3 + H2O
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cleavage with appearance of the alpha-chain
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complement component C3i + H2O
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cleavage of intact C3i (C3 with a reacted thiolester bond) by the MASP-1 CCP1-CCP2-SP fragment with a low but significant efficiency
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Fibrinogen + H2O
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rMASP1 cleavage of fibrinogen leads to the release of the proinflammatory peptide fibrinopeptide B. Catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
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?
fibrinogen + H2O
fibrin + ?
MASP-1-induced fibrin formation and activation is thrombin-dependent, in plasma environment fibrin formation is not directly induced by MASP-1 in the absence of prothrombin
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?
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
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mature coagulation factor XIII + ?
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proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
a noncomplement substrate, activation
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proform factor XIII + H2O
mature factor XIII + ?
the Val34 variant is a better substrate than the Leu34 variant
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mature mannan-binding lectin-associated serine protease 1 + ?
autocatalytic cleavage, a complement substrate, activation
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proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
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autocatalytic cleavage, a complement substrate, activation
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proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
autocatalytic cleavage
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?
mature mannan-binding lectin-associated serine protease 2 + ?
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proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
activation
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?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
a complement substrate, activation
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?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
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a complement substrate, activation
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?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
enzyme MASP-1 is the main activator of MASP-2
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mature mannan-binding lectin-associated serine protease 3 + ?
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proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
a complement substrate, activation
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mature thrombin-activatable fibrinolysis inhibitor + ?
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proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
activation
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protease activated receptor 4 + H2O
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PAR4, a noncomplement substrate, activation
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prothrombin + H2O
thrombin + ?
a noncomplement substrate, activation
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?
thrombin a + ?
enzyme MASP-1 cleaves prothrombinat three cleavage sites, MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393
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prothrombin + H2O
thrombin a + ?
enzyme MASP-1 cleaves prothrombinant three cleavage sites
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additional information
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complexes with mannose-binding lectin in the presence of Ca2+, involved in activation of complement cascade
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additional information
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involved in activation of complement cascade
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additional information
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involved in activation of complement cascade
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additional information
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involved in activation of complement cascade, circulates in serum complexed with mannose-binding protein
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additional information
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involved in activation of complement cascade, forms a complex with mannose-binding lectin
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additional information
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involved in activation of complement cascade, smallest functional unit for complement activation consists of serum mannose-binding protein dimers bound to MASP-1 homodimers
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additional information
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no cleavage of complement C4 by purified MASP-1
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additional information
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MASP-1 shows no activity toward complement C4. MASP-1 collaborates with MASP-2 in the generation of C3 convertase, a process observable at high serum concentration, but not at low serum concentration
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additional information
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autoactivation by cleavage of R448-/-I449. The enzyme is relatively unspecific
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additional information
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complement component C4, similar to C3, is basically resistant to the proteolytic activity of MASP-1. MASP-1 shows extreme Arg selectivity
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additional information
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MBL-MASP complexes, bound to mannan-agarose, generate clots when incubated with calcified plasma or purified fibrinogen and factor XIII
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additional information
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MASP-1 cannot cleave complement component C4, recombinant MASP-1 does not activate plasma prekallikrein
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additional information
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no activity with complement component C4. Direct activation of C3 convertase by MASP-1 occurs with very low catalytic efficiency and is not of physiological relevance
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additional information
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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
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additional information
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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
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additional information
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involved in activation of complement cascade
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additional information
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involved in activation of complement cascade
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additional information
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involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
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additional information
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involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
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additional information
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involved in activation of complement cascade, forms a complex with mannose-binding lectin
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additional information
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MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
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additional information
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MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
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additional information
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involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
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additional information
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involved in activation of complement cascade, circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a MASP homodimer bound to two mannose-binding protein trimeric subunits
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additional information
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no cleavage of complement C4 and N-alpha-carbobenzoxy-L-lysine p-nitropenhyl ester
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?