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Literature summary extracted from
- Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine (2017), Biochim. Biophys. Acta, 1865, 1123-1128 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.4.1.11 | - |
Citrobacter freundii |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.4.1.11 | mutant C115H, in complex with inhibitor L-norleucine, to 1.45 A resolution. The inhibotor binds both noncovalently and covalently at the active site, corresponding to the intermediates of the gamma- and beta-elimination reactions, Michaelis complex and the external aldimine | Citrobacter freundii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.4.1.11 | C115H | mutant is inactive in the gamma-elimination reaction of methionine while fully active in the gamma-elimination reaction of O-acetyl-L-homoserine and in the beta-elimination reaction of S-alk(en)yl-substituted cysteines | Citrobacter freundii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.4.1.11 | Citrobacter freundii | Q84AR1 | - |
- |
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