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Literature summary 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

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

Application

EC Number Application Comment Organism
3.4.21.B7 additional information MASP-1 enhances complement activation triggered by mannose-binding protein-MASP-2 complexes, but cannot initiate activation itself Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.B7 additional information MASP-1 ent, catalytically active form of MASP-1 produced by substituting residues 425Lys-His-Ile-Ser-Arg Rattus norvegicus
3.4.21.104 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

EC Number Inhibitors Comment Organism Structure
3.4.21.104 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.B7 8.9
-
 benzoyl-L-arginine p-nitroanilide cleavage by activated MASP-1 ent Rattus norvegicus
3.4.21.B7 13
-
 complement C2 cleavage by activated MASP-1 ent Rattus norvegicus
3.4.21.B7 13
-
 complement C2 complement component C2 Rattus norvegicus
3.4.21.104 additional information
-
 additional information recombinant MASP-2K: kinetics of free enzyme and enzyme complexed with myelin basic protein Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.104 extracellular
-
 Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.B7 complement component C2 + H2O Rattus norvegicus
-
 ?
-
 ?
3.4.21.104 complement component C2 + H2O Rattus norvegicus involved in activation of complement cascade 2 fragments of complement component C2
-
 ?
3.4.21.104 complement component C4 + H2O Rattus norvegicus involved in activation of complement cascade 2 fragments of complement C4
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.B7 Rattus norvegicus
-
-
-
3.4.21.104 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.104 glycoprotein
-
 Rattus norvegicus
3.4.21.104 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)

EC Number Purification (Comment) Organism
3.4.21.B7 by affinity chromatography Rattus norvegicus
3.4.21.104 MASP-2K mutant, inhibited in autoproteolytic activation, by affinity chromatography on an myelin basic protein-resin Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.21.104 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
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.104 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.B7 benzoyl-L-arginine p-nitroanilide + H2O
-
 Rattus norvegicus benzoyl-L-arginine + 4-nitroaniline
-
 ?
3.4.21.B7 complement component C2 + H2O
-
 Rattus norvegicus ?
-
 ?
3.4.21.B7 additional information no cleavage of complement C4 and N-alpha-carbobenzoxy-L-lysine p-nitropenhyl ester Rattus norvegicus ?
-
 ?
3.4.21.104 complement component C2 + H2O involved in activation of complement cascade Rattus norvegicus 2 fragments of complement component C2
-
 ?
3.4.21.104 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 ?
3.4.21.104 complement component C4 + H2O involved in activation of complement cascade Rattus norvegicus 2 fragments of complement C4
-
 ?
3.4.21.104 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

EC Number Synonyms Comment Organism
3.4.21.B7 MASP-1
-
 Rattus norvegicus
3.4.21.104 MASP-2
-
 Rattus norvegicus
3.4.21.104 MBP-associated serine protease-2
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.B7 3.9
-
 Complement component C2 cleavage by activated MASP-1 ent Rattus norvegicus
3.4.21.B7 4.3
-
 benzoyl-L-arginine p-nitroanilide cleavage by activated MASP-1 ent Rattus norvegicus