Crystallization (Comment) | Organism |
---|---|
structure to 1.6 A resolution. A single dimer of FrmB is observed in the asymmetric unit. The overall fold of FrmB is characteristic of the alpha/beta-hydrolase fold | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | Q2FUY3 | - |
- |
Staphylococcus aureus PS 47 | Q2FUY3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-D-lactoylglutathione + H2O | - |
Staphylococcus aureus | D-lactate + glutathione | - |
? | |
(S)-D-lactoylglutathione + H2O | - |
Staphylococcus aureus PS 47 | D-lactate + glutathione | - |
? | |
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O | i.e. POM-HEX, substrate is a prodrug of the compound HEX,which inhibits the glycolytic enzyme enolase | Staphylococcus aureus | [[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoic acid | - |
? | |
bis(pivaloyloxymethyl)(1-hydroxy-2-oxopiperidin-3-yl)phosphonate + H2O | i.e. POM-HEX, substrate is a prodrug of the compound HEX,which inhibits the glycolytic enzyme enolase | Staphylococcus aureus PS 47 | [[(hydroxymethoxy)(1-hydroxy-2-oxopiperidin-3-yl)phosphoryl]oxy]methyl 2,2-dimethylpropanoate + 2,2-dimethylpropanoic acid | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(2-methoxypropanoate) + H2O | - |
Staphylococcus aureus PS 47 | fluorescein-3'-oxymethyl 2-methoxypropanoate + 2-methoxypropanoate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O | - |
Staphylococcus aureus | fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(ethoxyacetate) + H2O | - |
Staphylococcus aureus PS 47 | fluorescein-3'-yoxymethyl ethoxyacetate + ethoxyacetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(methoxyacetate) + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl methoxyacetate + methoxyacetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis(propoxyacetate) + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl propoxyacetate + propoxyacetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis[(methylsulfanyl)acetate] + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl (methylsulfanyl)acetate + (methylsulfanyl)acetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene bis[[(propan-2-yl)sulfanyl]acetate] + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl [(propan-2-yl)sulfanyl]acetate + [(propan-2-yl)sulfanyl]acetate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene dibutanoate + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl butanoate + butanoate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene dihexanoate + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl hexanoate + hexanoate | - |
? | |
fluorescein-3',6'-bis(oxy)methylene dipentanoate + H2O | - |
Staphylococcus aureus | fluorescein-3'-oxymethyl pentanoate + pentanoate | - |
? | |
additional information | enzyme shows modest activity with substrates 4-nitrophenyl acetate, 4-nitrophenyl butanoate, but not with 4-nitrophenyl trimethylacetate | Staphylococcus aureus | ? | - |
- |
|
additional information | enzyme shows modest activity with substrates 4-nitrophenyl acetate, 4-nitrophenyl butanoate, but not with 4-nitrophenyl trimethylacetate | Staphylococcus aureus PS 47 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
? | x * 29500, calculated from sequence and SDS-PAGE | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
FrmB | - |
Staphylococcus aureus |
SAOUHSC_02962 | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
metabolism | FrmB activates the prodrug bis(pivaloyloxymethyl) (1-hydroxy-2-oxopiperidin-3-yl)phosphonate. Mutation of FrmB renders Staphylococcus aureus sensitive to bis(pivaloyloxymethyl) (1-hydroxy-2-oxopiperidin-3-yl)phosphonate | Staphylococcus aureus |
physiological function | FrmB has the highest activity toward oxygen ethers. FrmB hydrolyzes unbranched substrates with little regard for chain length or the end-of-chain bulk within the tested substrates. Branching at the position following the ester carbonyl is deleterious to FrmB activity. When oxygen is included in the chain, positioning at the beta-position to the carbonyl is strongly preferred over the gamma-position | Staphylococcus aureus |