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Literature summary for 4.2.2.1 extracted from

  • Jedrzejas, M.J.; Mewbourne, R.B.; Chantalat, L.; McPherson, D.T.
    Expression and purification of Streptococcus pneumoniae hyaluronate lyase from Escherichia coli (1998), Protein Expr. Purif., 13, 83-89.
    View publication on PubMed
Search for more literature for 4.2.2.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall the enzyme is anchored via its carboxy-terminal part to the pneumococcal cell wall by a covalent linkage with peptidoglycan structures Streptococcus pneumoniae 5618
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 1 * 80000, SDS-PAGE Streptococcus pneumoniae
83218
-
 x * 83218, calculation from nucleotide sequence Streptococcus pneumoniae
83280
-
 mass spectrometry experiments Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q54873
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Streptococcus pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hyaluronate
-
 Streptococcus pneumoniae alpha-4-deoxy-L-threo-hex-4-enopyranosyluronic acid-beta-1,3--N-acetyl-glucosamine
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 80000, SDS-PAGE Streptococcus pneumoniae
monomer x * 83218, calculation from nucleotide sequence Streptococcus pneumoniae