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Literature summary for 1.13.11.3 extracted from

  • Brown, C.K.; Vetting, M.W.; Earhart, C.A.; Ohlendorf, D.H.
    Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1 (2004), Annu. Rev. Microbiol., 58, 555-585.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Pseudomonas putida
-
Acinetobacter sp.

Protein Variants

Protein Variants Comment Organism
DELTA319-322 turnover-number is 4.14fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.1fold lower than that of the wild-type enzyme Acinetobacter sp.
R133H turnover-number is fold 500lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 1.8fold higher than that of the wild-type enzyme Acinetobacter sp.
R457S turnover-number is 1333fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.2fold lower than that of the wild-type enzyme Acinetobacter sp.
Y408C turnover-number is 523fold lower than that of the wild-type enzyme Pseudomonas putida
Y408E turnover-number is 6800fold lower than that of the wild-type enzyme Pseudomonas putida
Y408H turnover-number is 9714fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 10fold lower than that of the wild-type enzyme Pseudomonas putida
Y447H turnover-number is 567fold lower than that of the wild-type enzyme Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0029
-
3,4-dihydroxybenzoate mutant enzyme Y447H Pseudomonas putida
0.03
-
3,4-dihydroxybenzoate wild-type enzyme Pseudomonas putida
0.036
-
3,4-dihydroxybenzoate mutant enzyme R457S Acinetobacter sp.
0.038
-
3,4-dihydroxybenzoate mutant enzyme DELTA319-322 Acinetobacter sp.
0.056
-
O2 wild-type enzyme Pseudomonas putida
0.078
-
3,4-dihydroxybenzoate wild-type enzyme Acinetobacter sp.
0.142
-
3,4-dihydroxybenzoate mutant enzyme R133H Acinetobacter sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe3+ presence of a alphabetaFe3+ protomer in a variety of stoichiometries Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
-
-
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydroxybenzoate + O2
-
Pseudomonas putida 3-carboxy-cis,cis-muconate
-
?
3,4-dihydroxybenzoate + O2
-
Acinetobacter sp. 3-carboxy-cis,cis-muconate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.007
-
O2 mutant enzyme Y408H Pseudomonas putida
0.007
-
3,4-dihydroxybenzoate mutant enzyme Y408H Pseudomonas putida
0.01
-
O2 mutant enzyme Y408E Pseudomonas putida
0.01
-
3,4-dihydroxybenzoate mutant enzyme Y408E Pseudomonas putida
0.09
-
O2 mutant enzyme R457S Acinetobacter sp.
0.09
-
3,4-dihydroxybenzoate mutant enzyme R457S Acinetobacter sp.
0.12
-
O2 mutant enzyme Y447H Pseudomonas putida
0.12
-
3,4-dihydroxybenzoate mutant enzyme Y447H Pseudomonas putida
0.13
-
O2 mutant enzyme Y408C Pseudomonas putida
0.13
-
3,4-dihydroxybenzoate mutant enzyme Y408C Pseudomonas putida
0.24
-
O2 mutant enzyme R133H Acinetobacter sp.
0.24
-
3,4-dihydroxybenzoate mutant enzyme R133H Acinetobacter sp.
29
-
O2 mutant enzyme DELTA319-322 Acinetobacter sp.
29
-
3,4-dihydroxybenzoate mutant enzyme DELTA319-322 Acinetobacter sp.
68
-
O2 wild-type enzyme Pseudomonas putida
68
-
3,4-dihydroxybenzoate wild-type enzyme Pseudomonas putida
120
-
O2 wild-type enzyme Acinetobacter sp.
120
-
3,4-dihydroxybenzoate wild-type enzyme Acinetobacter sp.