Literature summary extracted from
Akhtar, M.S.; Bhakuni, V.
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
EC Number |
Application |
Comment |
Organism |
---|
4.2.2.1 |
pharmacology |
enzyme is a target for inhibitor design |
Streptococcus pneumoniae |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.2.1 |
overexpression of His-tagged enzyme in Escherichia coli |
Streptococcus pneumoniae |
General Stability
EC Number |
General Stability |
Organism |
---|
4.2.2.1 |
the C-terminal domain is less stable against thermal and guanidine hydrochloride denaturation than the N-terminal domain |
Streptococcus pneumoniae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.2.2.1 |
Ca2+ |
slight inhibition by 30% unfolding of the enzyme by ion binding |
Streptococcus pneumoniae |
|
4.2.2.1 |
guanidine hydrochloride |
strong inhibition, unfolding within 1 h |
Streptococcus pneumoniae |
|
4.2.2.1 |
guanidine isothiocyanate |
strong inhibition |
Streptococcus pneumoniae |
|
4.2.2.1 |
L-arginine |
strong inhibition |
Streptococcus pneumoniae |
|
4.2.2.1 |
L-arginine methyl ester |
strong inhibition |
Streptococcus pneumoniae |
|
4.2.2.1 |
Mg2+ |
slight inhibition by 30% unfolding of the enzyme by ion binding |
Streptococcus pneumoniae |
|
4.2.2.1 |
additional information |
no inhibition and conformational change induced by NaCl |
Streptococcus pneumoniae |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.2.2.1 |
41000 |
- |
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE |
Streptococcus pneumoniae |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.2.2.1 |
hyaluronan |
Streptococcus pneumoniae |
- |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.1 |
Streptococcus pneumoniae |
Q54873 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.2.1 |
isolated N-terminal domain from purified recombinant native enzyme |
Streptococcus pneumoniae |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.2.1 |
hyaluronan |
- |
Streptococcus pneumoniae |
? |
- |
? |
|
4.2.2.1 |
hyaluronan |
native enzyme and isolated N-terminal domain |
Streptococcus pneumoniae |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.2.1 |
? |
x * 41000, N-terminal domain, SDS-PAGE, x * 41000, C-terminal domain, SDS-PAGE |
Streptococcus pneumoniae |
4.2.2.1 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.2.1 |
spnHL |
- |
Streptococcus pneumoniae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
4.2.2.1 |
25 |
- |
assay at |
Streptococcus pneumoniae |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
4.2.2.1 |
additional information |
- |
transition temperatures |
Streptococcus pneumoniae |
4.2.2.1 |
55 |
- |
partially unfolding |
Streptococcus pneumoniae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.2.2.1 |
6 |
- |
assay at |
Streptococcus pneumoniae |