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Literature summary for 4.2.2.1 extracted from

  • Ponnuraj, K.; Jedrzejas, M.J.
    Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution (2000), J. Mol. Biol., 299, 885-895.
    View publication on PubMed

Application

Application Comment Organism
pharmacology enzyme is a target for development of antimicrobial agents Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme-disaccharide complex, X-ray diffraction structure determination and analysis at 1.7 A resolution, structure modeling Streptococcus pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, bridges between enzyme and substrate Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hyaluronan Streptococcus pneumoniae degradation leads to increased permeability of the host tissue and therefore helps bacterial invasion 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
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?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
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Reaction

Reaction Comment Organism Reaction ID
[hyaluronate]n = (4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine-[hyaluronate]n-m-1 + 2 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine + hyaluronate enzyme-product interaction from crystal structure, catalytic mechanism, interaction with substrate binding site, Tyr408, Asn349, and His399 are involved Streptococcus pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hyaluronan degradation leads to increased permeability of the host tissue and therefore helps bacterial invasion Streptococcus pneumoniae 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
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?
hyaluronic acid
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Streptococcus pneumoniae 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
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?