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Literature summary extracted from

  • Kudou, D.; Misaki, S.; Yamashita, M.; Tamura, T.; Esaki, N.; Inagaki, K.
    The role of cysteine 116 in the active site of the antitumor enzyme L-methionine gamma-lyase from Pseudomonas putida (2008), Biosci. Biotechnol. Biochem., 72, 1722-1730.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.11 expressed in Escherichia coli strain HB101 Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.11 C116A the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116D the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116E the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116F the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116G the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116H the mutant possesses little catalytic activity and shows marked increase in activity toward L-cysteine and a decrease in that toward L-methionine Pseudomonas putida
4.4.1.11 C116I the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116K the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116L the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116M the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116N the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116P the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116Q the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116R the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116S the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116T the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116V the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116W the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida
4.4.1.11 C116Y the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.11 propargylglycine
-
 Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4.1.11 0.11
-
 L-methionine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 0.12
-
 L-cysteine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 0.24
-
 DL-homocysteine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 0.39
-
 L-cysteine mutant enzyme C116A, at 37°C Pseudomonas putida
4.4.1.11 0.53
-
 L-cysteine wild type enzyme, at 37°C Pseudomonas putida
4.4.1.11 0.63
-
 L-cysteine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 0.92
-
 L-methionine wild type enzyme, at 37°C Pseudomonas putida
4.4.1.11 1.42
-
 L-methionine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 1.61
-
 DL-homocysteine mutant enzyme C116A, at 37°C Pseudomonas putida
4.4.1.11 1.8
-
 DL-homocysteine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 1.82
-
 DL-homocysteine wild type enzyme, at 37°C Pseudomonas putida
4.4.1.11 2.85
-
 L-methionine mutant enzyme C116A, at 37°C Pseudomonas putida

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.11 DEAE-Toyopearl 650M column chromatography and Sephacryl S-200 HR gel filtration Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.11 beta-chloro-L-alanine + H2O
-
 Pseudomonas putida ?
-
 ?
4.4.1.11 DL-homocysteine + H2O highest substrate specificity for DL-homocysteine Pseudomonas putida hydrogen sulfide + NH3 + 2-oxobutanoate
-
 ?
4.4.1.11 L-cysteine + H2O
-
 Pseudomonas putida sulfide + NH3 + pyruvate
-
 ?
4.4.1.11 L-ethionine + H2O
-
 Pseudomonas putida ethanethiol + NH3 + 2-oxobutanoate
-
 ?
4.4.1.11 L-methionine + H2O
-
 Pseudomonas putida methanethiol + NH3 + 2-oxobutanoate
-
 ?
4.4.1.11 additional information no activity with O-phospho-L-serine Pseudomonas putida ?
-
 ?
4.4.1.11 O-acetyl-L-serine + H2O weak activity Pseudomonas putida 2-oxopropanoate + NH3 + acetate
-
 ?
4.4.1.11 O-succinyl-L-homoserine + H2O weak activity Pseudomonas putida ?
-
 ?
4.4.1.11 S-ethyl-L-cysteine + H2O weak activity Pseudomonas putida ethanethiol + NH3 + 2-oxopropanoate
-
 ?
4.4.1.11 S-methyl-L-cysteine + H2O weak activity Pseudomonas putida methanethiol + NH3 + 2-oxopropanoate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.4.1.11 homotetramer
-
 Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
4.4.1.11 L-methionine gamma-lyase
-
 Pseudomonas putida
4.4.1.11 MGL
-
 Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.4.1.11 0.07
-
 L-methionine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 0.43
-
 L-cysteine mutant enzyme C116A, at 37°C Pseudomonas putida
4.4.1.11 0.57
-
 L-cysteine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 1.46
-
 L-methionine mutant enzyme C116A, at 37°C Pseudomonas putida
4.4.1.11 1.74
-
 DL-homocysteine mutant enzyme C116A, at 37°C Pseudomonas putida
4.4.1.11 1.77
-
 L-methionine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 2.27
-
 L-cysteine wild type enzyme, at 37°C Pseudomonas putida
4.4.1.11 2.59
-
 DL-homocysteine mutant enzyme C116S, at 37°C Pseudomonas putida
4.4.1.11 25.39
-
 L-methionine wild type enzyme, at 37°C Pseudomonas putida
4.4.1.11 30
-
 DL-homocysteine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 43.8
-
 L-cysteine mutant enzyme C116H, at 37°C Pseudomonas putida
4.4.1.11 44.84
-
 DL-homocysteine wild type enzyme, at 37°C Pseudomonas putida

Cofactor

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