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Literature summary for 3.4.21.104 extracted from

  • Chen, C.B.; Wallis, R.
    Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases (2004), J. Biol. Chem., 279, 26058-26065.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information autoactivation activity is enhanced by complex formation with myelin basic protein, thus myelin basic protein has a regulating function Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information construction of an enzymatically inactive enzyme, also not exhibiting autocatalytic activity, by substitution of the active size catalytic Ser residue with alanine, i.e. MASP-2A, construction of a zymogen with reduced autoproteolytic activity by substitution of the Arg residue at the autocatalytic cleavage site with lysine, i.e. MASP-2K Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
myelin basic protein no activity with substrate C4-component of the enzyme complexed with myelin basic protein before activation of the complex by binding to a suitable carbohydrate ligand Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information recombinant MASP-2K: kinetics of free enzyme and enzyme complexed with myelin basic protein Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
complement component C2 + H2O Rattus norvegicus involved in activation of complement cascade 2 fragments of complement component C2
-
?
complement component C4 + H2O Rattus norvegicus involved in activation of complement cascade 2 fragments of complement C4
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Rattus norvegicus
proteolytic modification autoproteolytic activation of the zymogen, cleavage site contains a Lys residue near the C-terminus, cleavage into 2 fragements, a larger N-termnal and a smaller C-terminal one, the latter contains the protease active site, autoactivation activity is enhanced by complex formation with myelin basic protein Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
MASP-2K mutant, inhibited in autoproteolytic activation, by affinity chromatography on an myelin basic protein-resin Rattus norvegicus

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) substrate recognition mechanism, mechanism of complement cascade activation Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C2 + H2O involved in activation of complement cascade Rattus norvegicus 2 fragments of complement component C2
-
?
complement component C2 + H2O only the activated enzyme binds to C2-component Rattus norvegicus 2 fragments of complement component C2 C2a and C2b fragments, preferred substrate ?
complement component C4 + H2O involved in activation of complement cascade Rattus norvegicus 2 fragments of complement C4
-
?
complement component C4 + H2O no activity of the enzyme complexed with myelin basic protein before complex activation by binding to a suitable carbohydrate ligand Rattus norvegicus 2 fragments of complement C4 C4a fragment, an N-terminal portion, and C4b fragment, the activated form ?

Synonyms

Synonyms Comment Organism
MASP-2
-
Rattus norvegicus
MBP-associated serine protease-2
-
Rattus norvegicus