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Literature summary for 4.4.1.11 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
Search for more literature for 4.4.1.11

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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

Inhibitors Comment Organism Structure
propargylglycine
-
 Pseudomonas putida

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P13254
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homotetramer
-
 Pseudomonas putida

Synonyms

Synonyms Comment Organism
L-methionine gamma-lyase
-
 Pseudomonas putida
MGL
-
 Pseudomonas putida

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Pseudomonas putida