Literature summary extracted from
Li, F.; Xu, D.
Functional role of R462 in the degradation of hyaluronan catalyzed by hyaluronate lyase from Streptococcus pneumoniae (2015), J. Mol. Model., 21, 196 .
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.2.2.1 |
R462A |
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462A can reduce the barrier height by about 2.8 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis |
Streptococcus pneumoniae |
4.2.2.1 |
R462Q |
modeling of site directed mutagenesis simulations of R462A and R462Q. The energetic profiles for the reaction processes are essentially the same as that in wild type enzyme, but the mutation accelerates the overall enzymatic activity. R462Q can reduce the barrier height by about 2.9 kcal/mol. The positive charge on the R462 guanidino side chain group plays a negative role in the catalysis |
Streptococcus pneumoniae |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.1 |
Streptococcus pneumoniae |
Q54873 |
serotype 4 |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.2.1 |
SP_0314 |
- |
Streptococcus pneumoniae |