Literature summary for 4.2.99.20 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.

Search for more literature for 4.2.99.20

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	A0A0H2WW38	-	-

Synonyms

Synonyms	Comment	Organism
MenH	-	Staphylococcus aureus

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Release 2023.1 (January 2023)