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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.
    View publication on PubMed

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