Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme in complex with inhibitor glycine, crystals are obtained using a method without the presence of ammonium sulfate, complexing with glycine by soaking of holoenzyme crystals in a cryoprotective mother liquid solution to which glycine is added stepwise from 5 mM to 20 mM during 20 min,, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement | Citrobacter freundii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glycine | competitive inhibitor, subtle conformational changes provide effective binding of the inhibitor and facilitate labilization of Calpha-protons of the external aldimine, binding structure, overview | Citrobacter freundii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-methionine + H2O | Citrobacter freundii | gamma-elimination reaction | methanethiol + NH3 + 2-oxobutanoate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter freundii | Q84AR1 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate | gamma-elimination reaction mechanism and intermediates, overview | Citrobacter freundii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-methionine + H2O | gamma-elimination reaction | Citrobacter freundii | methanethiol + NH3 + 2-oxobutanoate | - |
? | |
L-methionine + H2O | gamma-elimination reaction, initial aldimine, quinonoid, and ketimine intermediates of the gamma-elimination reaction, possible concerted mechanisms of reversible ketimine formation and pro-(R)-Calpha-proton exchange, overview | Citrobacter freundii | methanethiol + NH3 + 2-oxobutanoate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MGL | - |
Citrobacter freundii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Citrobacter freundii |
General Information | Comment | Organism |
---|---|---|
additional information | catalytic residues: Lys210 is the base, and Tyr113 acts as a general acid, active site structure, overview | Citrobacter freundii |