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Literature summary for 3.2.1.49 extracted from

  • Hsieh, H.Y.; Calcutt, M.J.; Chapman, L.F.; Mitra, M.; Smith, D.S.
    Purification and characterization of a recombinant alpha-N-acetylgalactosaminidase from Clostridium perfringens (2003), Protein Expr. Purif., 32, 309-316.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the gene encoding the clostridial enzyme is cloned in an Escherichia coli T7 expression system Clostridium perfringens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide pH 6.5, 37°C, recombinant enzyme Clostridium perfringens
1.62
-
o-nitrophenyl-N-acetyl-alpha-D-galactosaminide pH 6.5, 37°C, recombinant enzyme Clostridium perfringens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
719600
-
x * 719600, denatured recombinant enzyme, x * 724200, native recombinant enzyme, SDS-PAGE Clostridium perfringens
724200
-
x * 719600, denatured recombinant enzyme, x * 724200, native recombinant enzyme, SDS-PAGE Clostridium perfringens

Organism

Organism UniProt Comment Textmining
Clostridium perfringens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Clostridium perfringens

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
84.11
-
-
Clostridium perfringens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is highly selective for terminal N-acetylgalactosamine residues, sugars other than N-acetyl-alpha-D-galactosaminide are no substrates Clostridium perfringens ?
-
?
o-nitrophenyl N-acetyl-alpha-D-galactosaminide + H2O substrate from the blood type A2 antigen producing H antigen, blood type O Clostridium perfringens o-nitrophenol + N-acetyl-alpha-D-galactosamine
-
?
p-nitrophenyl-N-acetyl-alpha-D-galactosaminide + H2O
-
Clostridium perfringens p-nitrophenol + N-acetyl-alpha-D-galactosamine
-
?

Subunits

Subunits Comment Organism
? x * 719600, denatured recombinant enzyme, x * 724200, native recombinant enzyme, SDS-PAGE Clostridium perfringens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4 45
-
Clostridium perfringens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7 recombinant enzyme Clostridium perfringens

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8
-
Clostridium perfringens