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Literature summary extracted from

  • Sato, D.; Shiba, T.; Yunoto, S.; Furutani, K.; Fukumoto, M.; Kudou, D.; Tamura, T.; Inagaki, K.; Harada, S.
    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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.11
-
 Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.11 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

EC Number Protein Variants Comment Organism
4.4.1.11 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

EC Number Organism UniProt Comment Textmining
4.4.1.11 Pseudomonas putida P13254
-
-

Synonyms

EC Number Synonyms Comment Organism
4.4.1.11 MdeA
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.11 pyridoxal 5'-phosphate
-
 Pseudomonas putida