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Literature summary for 4.2.2.1 extracted from
- Streptococcus pneumoniae hyaluronate lyase contains two non-cooperative independent folding/unfolding structural domains: characterization of functional domain and inhibitors of enzyme (2003), J. Biol. Chem., 278, 25509-25516.
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | enzyme is a target for inhibitor design | Streptococcus pneumoniae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of His-tagged enzyme in Escherichia coli | Streptococcus pneumoniae |
General Stability
| General Stability | Organism |
|---|---|
| the C-terminal domain is less stable against thermal and guanidine hydrochloride denaturation than the N-terminal domain | Streptococcus pneumoniae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | slight inhibition by 30% unfolding of the enzyme by ion binding | Streptococcus pneumoniae |  |
| guanidine hydrochloride | strong inhibition, unfolding within 1 h | Streptococcus pneumoniae | |
| guanidine isothiocyanate | strong inhibition | Streptococcus pneumoniae | |
| L-arginine | strong inhibition | Streptococcus pneumoniae | |
| L-arginine methyl ester | strong inhibition | Streptococcus pneumoniae | |
| Mg2+ | slight inhibition by 30% unfolding of the enzyme by ion binding | Streptococcus pneumoniae | |
| additional information | no inhibition and conformational change induced by NaCl | Streptococcus pneumoniae |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE | Streptococcus pneumoniae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hyaluronan | Streptococcus pneumoniae | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptococcus pneumoniae | Q54873 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| isolated N-terminal domain from purified recombinant native enzyme | Streptococcus pneumoniae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hyaluronan | - |
Streptococcus pneumoniae | ? | - |
? | |
| hyaluronan | native enzyme and isolated N-terminal domain | Streptococcus pneumoniae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE | Streptococcus pneumoniae |
| More | enzyme consists of 2 structural domains, C-terminal and N-terminal, each of which folds and unfolds independent from the other due to lack of cooperative interactions between them, structure determination | Streptococcus pneumoniae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| spnHL | - |
Streptococcus pneumoniae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Streptococcus pneumoniae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
transition temperatures | Streptococcus pneumoniae |
| 55 | - |
partially unfolding | Streptococcus pneumoniae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Streptococcus pneumoniae |
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Release 2023.1 (January 2023)
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