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Literature summary for 4.4.1.11 extracted from
- Structural and mechanistic insights into homocysteine degradation by a mutant of methionine gamma-lyase based on substrate-assisted catalysis (2017), Protein Sci., 26, 1224-1230 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Pseudomonas putida |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in mutant C116H a loop structure (Ala51-Asn64) in the adjacent subunit of the catalytic dimer cannot approach the cofactor pyridoxal 5'-phosphate because His116 disrupts the interaction of Asp241 with Lys240, and the liberated side chain of Lys240 causes steric hindrance with this loop | Pseudomonas putida |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C116H | mutation renders the enzyme inactive towards L-methionine, but activity is restored when the substrate is homocysteine due to substrate-assisted catalysis | Pseudomonas putida |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | P13254 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MdeA | - |
Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Pseudomonas putida |  |
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