Literature summary extracted from
Dawson, A.; Fyfe, P.; Gillet, F.; Hunter, W.
Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity (2011), BMC Struct. Biol., 11, 19.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.99.20 |
expression in Escherichia coli |
Staphylococcus aureus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.99.20 |
to 2 A resolution. The overall basic active site displays pronounced hydrophobic character on one side and these properties complement those of the substrate. A complex network of hydrogen bonds involving well-ordered water molecules serves to position key residues participating in the recognition of substrate and subsequent catalysis. Proton shuttle mechanism, reliant on a catalytic triad consisting of Ser89, Asp216 and His243. The reaction is initiated by proton abstraction from the substrate by an activated Ser89. The propensity to form a conjugated system provides the driving force for pyruvate elimination. During the elimination, a methylene group is converted to a methyl and probybly His243 provides a proton, previously acquired from Ser89 for reduction. A conformational change of the protonated His243 may be encouraged by the presence of an anionic intermediate in the active site |
Staphylococcus aureus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.99.20 |
Staphylococcus aureus |
A0A0H2WW38 |
- |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.99.20 |
MenH |
- |
Staphylococcus aureus |