BRENDA - Enzyme Database show
show all sequences of 3.4.21.104

Serine proteases of the classical and lectin pathways: similarities and differences

Gal, P.; Barna, L.; Kocsis, A.; Zavodszky, P.; Immunobiology 212, 267-277 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
Homo sapiens
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
Rattus norvegicus
Crystallization (Commentary)
Crystallization
Organism
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
-
Homo sapiens
C1-inhibitor
-
Homo sapiens
C1-inhibitor
-
Rattus norvegicus
additional information
MASP-3 might be able to downregulate MASP-2 activity
Homo sapiens
additional information
MASP-3 might be able to downregulate MASP-2 activity
Rattus norvegicus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2; required for dimerization
Homo sapiens
Ca2+
Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
complement component C2 + H2O
Homo sapiens
-
?
-
-
?
complement component C2 + H2O
Rattus norvegicus
-
?
-
-
?
complement component C4 + H2O
Homo sapiens
-
?
-
-
?
complement component C4 + H2O
Rattus norvegicus
-
?
-
-
?
additional information
Homo sapiens
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
?
-
-
-
additional information
Rattus norvegicus
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
no glycoprotein
-
Homo sapiens
proteolytic modification
the enzyme performs autoactivation, C4 binding to the zymogen stabilizes the activating enzyme, overview
Homo sapiens
proteolytic modification
the enzyme performs autoactivation
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
complement component C2 + H2O
-
680105
Homo sapiens
?
-
-
-
?
complement component C2 + H2O
-
680105
Rattus norvegicus
?
-
-
-
?
complement component C4 + H2O
-
680105
Homo sapiens
?
-
-
-
?
complement component C4 + H2O
-
680105
Rattus norvegicus
?
-
-
-
?
additional information
substrate specificity, overview
680105
Rattus norvegicus
?
-
-
-
-
additional information
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
680105
Homo sapiens
?
-
-
-
-
additional information
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
680105
Rattus norvegicus
?
-
-
-
-
additional information
substrate specificity, overview, no activity with gelatin, the enzyme performs proteolytic autoactivation, the N-terminal third of MASP-2, i.e. MAp19 or sMAp, comprises the CUB1 and EGF modules of MASP-2 plus an extra C-terminal EQSL tetrapeptide, which is encoded by a separate exon, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive
680105
Homo sapiens
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
; Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, even though they share the same N-terminal domains
Homo sapiens
dimer
Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, eventhough they share the same N-terminal domains
Rattus norvegicus
More
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, the very flexible C-terminal catalytic SP region shows a typical chymotrypsin fold with two six-stranded beta-barrels with the catalytic triad located at the junction of the to barrels and formed by Ser195, His57, and Asp102, active site structure, overview
Homo sapiens
More
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview
Rattus norvegicus
Cloned(Commentary) (protein specific)
Commentary
Organism
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
Homo sapiens
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview
Rattus norvegicus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
-
Homo sapiens
C1-inhibitor
-
Homo sapiens
C1-inhibitor
-
Rattus norvegicus
additional information
MASP-3 might be able to downregulate MASP-2 activity
Homo sapiens
additional information
MASP-3 might be able to downregulate MASP-2 activity
Rattus norvegicus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2; required for dimerization
Homo sapiens
Ca2+
Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
complement component C2 + H2O
Homo sapiens
-
?
-
-
?
complement component C2 + H2O
Rattus norvegicus
-
?
-
-
?
complement component C4 + H2O
Homo sapiens
-
?
-
-
?
complement component C4 + H2O
Rattus norvegicus
-
?
-
-
?
additional information
Homo sapiens
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
?
-
-
-
additional information
Rattus norvegicus
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
no glycoprotein
-
Homo sapiens
proteolytic modification
the enzyme performs autoactivation, C4 binding to the zymogen stabilizes the activating enzyme, overview
Homo sapiens
proteolytic modification
the enzyme performs autoactivation
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
complement component C2 + H2O
-
680105
Homo sapiens
?
-
-
-
?
complement component C2 + H2O
-
680105
Rattus norvegicus
?
-
-
-
?
complement component C4 + H2O
-
680105
Homo sapiens
?
-
-
-
?
complement component C4 + H2O
-
680105
Rattus norvegicus
?
-
-
-
?
additional information
substrate specificity, overview
680105
Rattus norvegicus
?
-
-
-
-
additional information
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
680105
Homo sapiens
?
-
-
-
-
additional information
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
680105
Rattus norvegicus
?
-
-
-
-
additional information
substrate specificity, overview, no activity with gelatin, the enzyme performs proteolytic autoactivation, the N-terminal third of MASP-2, i.e. MAp19 or sMAp, comprises the CUB1 and EGF modules of MASP-2 plus an extra C-terminal EQSL tetrapeptide, which is encoded by a separate exon, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive
680105
Homo sapiens
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
; Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, even though they share the same N-terminal domains
Homo sapiens
dimer
Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, eventhough they share the same N-terminal domains
Rattus norvegicus
More
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, the very flexible C-terminal catalytic SP region shows a typical chymotrypsin fold with two six-stranded beta-barrels with the catalytic triad located at the junction of the to barrels and formed by Ser195, His57, and Asp102, active site structure, overview
Homo sapiens
More
enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview
Rattus norvegicus
Other publictions for EC 3.4.21.104
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
731745
Keizer
TFPI inhibits lectin pathway o ...
Homo sapiens
Eur. J. Immunol.
45
544-550
2015
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1
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1
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1
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731780
Asgari
Mannan-binding lectin-associat ...
Mus musculus
FASEB J.
28
3996-4003
2014
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3
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1
1
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732518
Parej
Dissociation and re-associatio ...
Homo sapiens
Mol. Immunol.
59
1-9
2014
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1
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1
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1
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1
1
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732265
Degn
Co-complexes of MASP-1 and MAS ...
Homo sapiens
J. Immunol.
191
1334-1345
2013
-
-
1
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-
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1
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1
1
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718122
Duncan
Multiple domains of MASP-2, an ...
Homo sapiens
Mol. Immunol.
49
593-600
2012
-
-
1
-
1
-
1
1
-
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1
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1
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1
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1
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4
1
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2
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1
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1
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1
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1
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1
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1
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1
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4
1
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2
-
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-
1
1
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732057
Heja
Monospecific inhibitors show t ...
Homo sapiens
J. Biol. Chem.
287
20290-20300
2012
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1
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2
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1
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2
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718181
Novovic
Mannan-binding lectin and mann ...
Homo sapiens
Pancreas
40
1097-1102
2011
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-
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1
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1
1
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708201
Miller
Molecular defects in the manno ...
Homo sapiens
Clin. Mol. Allergy
8
6-6
2010
-
-
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1
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2
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1
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1
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1
1
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708697
Gulla
Activation of mannan-binding l ...
Homo sapiens
Immunology
129
482-495
2010
2
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2
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1
4
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1
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1
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1
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4
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709084
Venkatraman Girija
Engineering novel complement a ...
Rattus norvegicus
J. Biol. Chem.
285
10546-10552
2010
2
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1
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1
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709160
Skjoedt
A novel mannose-binding lectin ...
Homo sapiens
J. Biol. Chem.
285
8234-8243
2010
-
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2
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2
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2
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1
1
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717934
Kocsis
Selective inhibition of the le ...
Homo sapiens
J. Immunol.
185
4169-4178
2010
-
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1
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4
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1
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1
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1
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1
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1
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3
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1
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2
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700247
Swierzko
Mannan-binding lectin-associat ...
Homo sapiens
Mol. Immunol.
46
1696-1701
2009
-
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1
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1
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1
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700576
Zehnder
Prognosis in pediatric hematol ...
Homo sapiens
Pediatr. Blood Cancer
53
53-57
2009
-
1
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2
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1
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Wallis
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Walsh
Fluorochrome-linked immunoassa ...
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683990
Krarup
Simultaneous activation of com ...
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684060
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665232
Verma
Clinical significance of manno ...
Homo sapiens
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Nakao
Lectin pathway of bony fish co ...
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Gal
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