1.13.11.3: protocatechuate 3,4-dioxygenase
This is an abbreviated version!
For detailed information about protocatechuate 3,4-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.3
-
1.13.11.3
-
catecholate
-
1,2-dioxygenase
-
intradiol
-
4-hydroxybenzoate
-
3,4-dihydroxybenzoate
-
beta-ketoadipate
-
ring-cleavage
-
gentisate
-
beta-carboxy-cis,cis-muconate
-
enol-lactone
-
hydroxyquinol
-
orville
-
lipscomb
-
fuscum
-
cis-muconate
-
4-methylcatechols
-
3,5-di-tert-butylcatechol
-
analysis
-
environmental protection
-
degradation
- 1.13.11.3
-
catecholate
-
1,2-dioxygenase
-
intradiol
- 4-hydroxybenzoate
- 3,4-dihydroxybenzoate
-
beta-ketoadipate
-
ring-cleavage
- gentisate
- beta-carboxy-cis,cis-muconate
-
enol-lactone
- hydroxyquinol
-
orville
-
lipscomb
- fuscum
-
cis-muconate
- 4-methylcatechols
- 3,5-di-tert-butylcatechol
- analysis
- environmental protection
- degradation
Reaction
Synonyms
3,4-PCase, 3,4-PCD, 3,4-PCDase, 3,4-POD, EC 1.13.1.3, EC 1.99.2.3, More, oxygenase, protocatechuate 3,4-di-, P3,4DO, P3,4O enzyme, P34O, PCA 3,4-dioxygenase, PcaG, PcaH, PcaHG, PCD, protocatchetuate 3,4-dioxygenase, protocatechuate 3,4-dioxygenase, protocatechuate oxygenase, protocatechuic 3,4-dioxygenase, protocatechuic 3,4-oxygenase, protocatechuic acid oxidase
ECTree
1.13.11.3 protocatechuate 3,4-dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.3 - protocatechuate 3,4-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
R133H
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
R133H
-
gain of function mutation confers catechol 1,2-dioxygenase activity
-
R142K
-
like wild-type no acticity of mutated protocatechuate 3,4-dioxygenase I with 4-sulfocatechol
R142K/W153V
-
protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
R153V
-
protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
Y408C
Y408E
Y408F
-
iron is not tightly bound, the Y408F mutant does not reconstitute above half-occupancy and loses color during crystallization attempts. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
Y408H
Y447H
additional information
R133H
-
gain of function mutation confers catechol 1,2-dioxygenase activity
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
Y408C
-
turnover-number is 523fold lower than that of the wild-type enzyme
Y408C
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
Y408E
-
turnover-number is 6800fold lower than that of the wild-type enzyme
Y408E
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation.
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
Y408H
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
Y447H
-
turnover-number is 567fold lower than that of the wild-type enzyme
additional information
-
mutants are constructed so that their pcaG genes contained variations in repeat sequence capable of producing a selectable phenotype following a specific deletion. Deletion frequencies of the various mutations is determined and compared with repair frequencies of three different single-base mutations.
additional information
-
immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations
additional information
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
additional information
-
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
additional information
-
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
-
