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Literature summary for 3.4.21.104 extracted from

  • Harmat, V.; Gal, P.; Kardos, J.; Szilagyi, K.; Ambrus, G.; Vegh, B.; Naray-Szabo, G.; Zavodszky, P.
    The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions (2004), J. Mol. Biol., 342, 1533-1546.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of the catalytic fragment encompassing the second complement control protein module and the serine protease domain, i.e. MASP-2-CCP2-SP, in Escherichia coli strain BL21(DE3), the recombinant construct contains an extra-tetrapeptide ASMT at the N-terminus Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
catalytic fragment encompassing the second complement control protein module and the serine protease domain, in presence of Na+, in absence of Mg2+, 0.8 mg/ml purified recombinant protein in 140 mM NaCl, 20 mM Tris-HCl, pH 7.4, and 0.05% w/v NaN3, hanging drop vapour diffusion method at 20°C, mixing with equal volume of reservoir solution containing 30% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, 0.1 M Tris-HCl, pH 7.5, X-ray diffraction structure determination and analysis at 2.25 A resolution Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by Na+ Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no induction by Na+ 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
-
2 fragments of complement component C2
-
?
complement component C4 + H2O Homo sapiens
-
2 fragments of complement C4
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92876
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no glycoprotein
-
Homo sapiens
proteolytic modification autoactivation Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant catalytic fragment encompassing the second complement control protein module and the serine protease domain, i.e. MASP-2-CCP2-SP, from Escherichia coli strain BL21(DE3) Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile) structure-function analysis of the catalytic unit, enzyme-substrate interaction is different from enzyme C1 which has the same substrate specificity, MASP-2 shows a subsite flexibility in substrate specificity, catalytic residues are Asp526 and His525, active site structure, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4,4'-dithiopyridine + H2O
-
Homo sapiens ?
-
?
alpha-N-benzyloxycarbonyl-L-lysine thiobenzyl ester + H2O
-
Homo sapiens ?
-
?
complement component C2 + H2O
-
Homo sapiens 2 fragments of complement component C2
-
?
complement component C4 + H2O
-
Homo sapiens 2 fragments of complement C4
-
?
complement component C4 + H2O the complement control protein CCP module is essential for cleavage Homo sapiens 2 fragments of complement C4
-
?

Subunits

Subunits Comment Organism
More enzyme surface segment analysis, structure-function analysis Homo sapiens

Synonyms

Synonyms Comment Organism
mannose-binding lectin-associated serine protease-2
-
Homo sapiens
MASP-2
-
Homo sapiens
MBL-associated serine protease-2
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Homo sapiens