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Literature summary for 4.1.1.76 extracted from

  • Miyazaki, M.; Kakidani, H.; Hanzawa, S.; Ohta, H.
    Cysteine 188 revealed as being critical for the enzyme acticity of arylmalonate decarboxylase by site-directed mutagenesis (1997), Biol. Chem. Soc. Jpn., 70, 2765-2769.
No PubMed abstract available
Search for more literature for 4.1.1.76

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser expressed in Escherichia coli Bordetella bronchiseptica

Protein Variants

Protein Variants Comment Organism
C101S mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre Bordetella bronchiseptica
C148S mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre Bordetella bronchiseptica
C171S mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre Bordetella bronchiseptica
C188S mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser. CD spectra indicate that the conformational differences of Cys101Ser and Cys188Ser compared to that of the native enzyme are not significant. Only Cys188Ser shows a drastic decrease in enzyme activity, indicating that Cys188 is located at the active centre Bordetella bronchiseptica

Inhibitors

Inhibitors Comment Organism Structure
alpha-Bromophenylacetic acid
-
 Bordetella bronchiseptica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3
-
 alpha-phenylmalonate mutant enzyme Cys101Ser Bordetella bronchiseptica
4.9
-
 alpha-phenylmalonate mutant enzyme Cys188Ser Bordetella bronchiseptica
9.1
-
 alpha-phenylmalonate mutant enzyme Cys171Ser Bordetella bronchiseptica
11.5
-
 alpha-phenylmalonate mutant enzyme Cys148Ser Bordetella bronchiseptica
13.3
-
 alpha-phenylmalonate wild-type enzyme Bordetella bronchiseptica

Organism

Organism UniProt Comment Textmining
Bordetella bronchiseptica
-
 mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser Bordetella bronchiseptica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Phenylmalonate
-
 Bordetella bronchiseptica Phenylacetate + CO2
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 wild-type enzyme, half-life: 32 min Bordetella bronchiseptica
50
-
 mutant enzymes Cys101Ser, Cys148Ser, Cys171Ser and Cys188Ser, half-life: 12-19 min Bordetella bronchiseptica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.62
-
 alpha-phenylmalonate mutant enzyme Cys188Ser Bordetella bronchiseptica
62.3
-
 alpha-phenylmalonate mutant enzyme Cys171Ser Bordetella bronchiseptica
100
-
 alpha-phenylmalonate mutant enzyme Cys148Ser Bordetella bronchiseptica
248
-
 alpha-phenylmalonate mutant enzyme Cys101Ser Bordetella bronchiseptica
366
-
 alpha-phenylmalonate wild-type enzyme Bordetella bronchiseptica