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Literature summary for 4.2.2.1 extracted from

  • Li, S.; Taylor, K.B.; Kelly, S.J.; Jedrzejas, M.J.
    Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase (2001), J. Biol. Chem., 276, 15125-15130.
    View publication on PubMed
Search for more literature for 4.2.2.1

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme complexed with L-ascorbic acid, X-ray diffraction structure determination and analysis at 2.0 A resolution Streptococcus pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
L-ascorbic acid i.e. vitamin C, reversible, competitive, one molecule binds to the active site of all 3 catalytic positions, interacts with enzyme residues R243, N290, W292, Y408, R462, R466, and N580, inhibits the invasion and spreading of the bacterium in tissues in vivo Streptococcus pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q54873
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hyaluronan
-
 Streptococcus pneumoniae 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
-
 ?

Synonyms

Synonyms Comment Organism
spreading factor
-
 Streptococcus pneumoniae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Streptococcus pneumoniae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Streptococcus pneumoniae