Literature summary extracted from
Li, S.; Kelly, S.J.; Lamani, E.; Ferraroni, M.; Jedrzejas, M.J.
Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase (2000), EMBO J., 19, 1228-1240.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.2.1 |
overexpression of fully functional truncated wild-type and mutant enzymes in Escherichia coli |
Streptococcus pneumoniae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.2.1 |
purified recombinant truncated wid-type enzyme and selenomethionine derivative, comprising residues Ala168-Ala893, in 3.5 M ammonium sulfate, 200 mM sodium cacodylate, pH 6.0, cryoprotection in 30% xylitol, heavy atom derivative X-ray diffraction structure determination and analysis at 1.56 A resolution |
Streptococcus pneumoniae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.2.2.1 |
H399A |
site-directed mutagenesis, highly reduced activity compared to wild-type enzyme |
Streptococcus pneumoniae |
4.2.2.1 |
N349A |
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme |
Streptococcus pneumoniae |
4.2.2.1 |
N580G |
site-directed mutagenesis, slightly increased activity compared to wild-type enzyme |
Streptococcus pneumoniae |
4.2.2.1 |
R243V |
site-directed mutagenesis, reduced activity compared to the wild-type enzyme |
Streptococcus pneumoniae |
4.2.2.1 |
Y408F |
site-directed mutagenesis, inactive mutant |
Streptococcus pneumoniae |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.2.2.1 |
Ca2+ |
binding modulates enzyme structure |
Streptococcus pneumoniae |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.1 |
Streptococcus pneumoniae |
- |
- |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
4.2.2.1 |
[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 |
catalytic mechanism, substrate binding, structure modeling, residues Tyr408, Asn349, and His399 are involved in catalysis and important |
Streptococcus pneumoniae |
|
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.2.1 |
hyaluronan |
- |
Streptococcus pneumoniae |
3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.2.1 |
More |
N-terminal alpha- and C-terminal beta-domain structure determination, determination of interface residues, overview |
Streptococcus pneumoniae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.2.1 |
bacterial spreading factor |
- |
Streptococcus pneumoniae |
4.2.2.1 |
spnHL |
- |
Streptococcus pneumoniae |