Any feedback?
Literature summary for 4.2.2.1 extracted from
- Catalytic mechanism of hyaluronate lyase from Spectrococcus pneumonia: quantum mechanical/molecular mechanical and density functional theory studies (2013), J. Phys. Chem. B, 117, 10161-10172.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Streptococcus pneumoniae | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Streptococcus pneumoniae |  |
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 | binding of the substrate molecule can lead to the ionization of Y408 and protonation of H399, Y408 serves as the general base in the proton abstraction, while general acid is the next proton donation step. The reaction can be classified into syn elimination reaction mechanism, reaction mechanism analysis, detailed 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 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| spnHL | - |
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 |
| additional information | complete catalytic cycle for the degradation of hyaluronan tetrasaccharide catalyzed by the hyaluronate lyase from Spectrococcus pneumonia, overview. Active site residue is tyrosine 408. Quantum mechanical/molecular mechanical and desity calculation and modeling using truncated active site models | Streptococcus pneumoniae |
| physiological function | major function of the enzyme is to degrade hyaluronic acid | Streptococcus pneumoniae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
