Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Streptococcus pneumoniae | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptococcus pneumoniae | - |
- |
- |
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 | 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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | the enzyme belongs to PL subfamily 8, which has an overall alpha/alpha + beta architecture | Streptococcus pneumoniae |
Synonyms | Comment | Organism |
---|---|---|
spnHL | - |
Streptococcus pneumoniae |
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 |