Literature summary extracted from
Kudou, D.; Misaki, S.; Yamashita, M.; Tamura, T.; Takakura, T.; Yoshioka, T.; Yagi, S.; Hoffman, R.M.; Takimoto, A.; Esaki, N.; Inagaki, K.
Structure of the antitumour enzyme L-methionine gamma-lyase from Pseudomonas putida at 1.8 A resolution (2007), J. Biochem., 141, 535-544.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.4.1.11 |
1.8 A resolution. Residues Y59 and R61 of neighbouring subunits contact the phosphate group of pyridoxal 5-phosphate. Residues K240, D241 and R61 of one partner monomer and Y114 and C116 of the other form a hydrogen-bond network in the active site |
Pseudomonas putida |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.4.1.11 |
C116S |
9% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
C116T |
40% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
F128C |
112% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
G9C/D385C |
46% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
L341H |
9% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
R61A |
1% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
R61E |
no activity |
Pseudomonas putida |
4.4.1.11 |
R61F |
2% of wild-type activity |
Pseudomonas putida |
4.4.1.11 |
S248C |
131% of wild-type activity |
Pseudomonas putida |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.4.1.11 |
Pseudomonas putida |
P13254 |
- |
- |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.4.1.11 |
pyridoxal 5'-phosphate |
- |
Pseudomonas putida |
|