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Literature summary for 3.4.21.104 extracted from

  • Gal, P.; Barna, L.; Kocsis, A.; Zavodszky, P.
    Serine proteases of the classical and lectin pathways: similarities and differences (2007), Immunobiology, 212, 267-277.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) 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 (Comment) Organism
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis Homo sapiens

Inhibitors

Inhibitors Comment 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 Comment Organism Structure
Ca2+ 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 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
Homo sapiens
proteolytic modification the enzyme performs autoactivation Rattus norvegicus
proteolytic modification the enzyme performs autoactivation, C4 binding to the zymogen stabilizes the activating enzyme, overview 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
-
Rattus norvegicus ?
-
?
complement component C4 + H2O
-
Homo sapiens ?
-
?
complement component C4 + H2O
-
Rattus norvegicus ?
-
?
additional information substrate specificity, overview 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 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 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 Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Homo sapiens
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, overview 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

Synonyms

Synonyms Comment Organism
MASP-2
-
Homo sapiens
MASP-2
-
Rattus norvegicus
MASP-2 protein of the lectin pathway, can autoactivate and cleaves complements C2 and C4 Homo sapiens