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Literature summary for 4.2.2.1 extracted from

  • Zheng, M.; Zhang, H.; Xu, D.
    Initial events in the degradation of hyaluronan catalyzed by hyaluronate lyase from Spectrococcus pneumoniae: QM/MM simulation (2012), J. Phys. Chem. B, 116, 11166-11172.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Streptococcus pneumoniae
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-

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

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 along with the substrate binding, the phenylhydroxyl hydrogen atom of Tyr408 will transfer to nearby His399 via a near barrierless transition state, which results in a negatively charged Tyr408 and positively charged His399. The Tyr408, rather than the previously proposed His399, acts as the general base for the subsequent beta-elimination reaction. The His399 has the function of neutralizing the C5-carboxyl group, reaction mechanism, overview Streptococcus pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hyaluronic acid nonhydrolytic cleavage of the glycosidic bond, initiation of degradation activity analysis by molecular mechanical molecular dynamic simulations and free energy profiles, simulation and analysis of the enzyme-substrate complex structure, overview Streptococcus pneumoniae ?
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?

Subunits

Subunits Comment Organism
trimer the enzyme belongs to PL subfamily 8, which has an overall alpha/alpha + beta architecture Streptococcus pneumoniae

Synonyms

Synonyms Comment Organism
spnHL
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Streptococcus pneumoniae

General Information

General Information Comment Organism
evolution the enzyme belongs to PL subfamily 8, which has an overall alpha/alpha + beta architecture Streptococcus pneumoniae
physiological function major function of the enzyme is to degrade hyaluronic acid Streptococcus pneumoniae