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2,3-dihydroxybenzoate + O2
?
2,4-dihydroxybenzoate + O2
?
2,5-dihydroxybenzoate + O2
?
2,6-dihydroxybenzoate + O2
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
3,4-dihydroxybenzoate + O2
?
3,4-dihydroxybenzoate + O2
beta-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
3,4-dihydroxymandelic acid + O2
?
3,4-dihydroxyphenylacetate + O2
?
3,4-dihydroxyphenylalanine + O2
?
Nocardia erythropolis
-
at 10.7% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylpropionic acid + O2
?
-
-
-
-
?
3,5-dihydroxybenzoate + O2
?
3-(3,4-dihydroxyphenyl)propionate + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3-methylcatechol + O2
2-methylmuconate
4-cresol + O2
?
-
-
-
-
?
4-hydroxybenzoic acid + O2
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
4-methylcatechol + O2
?
-
-
-
-
?
4-sulfocatechol + O2
3-sulfomuconate
5-fluoro-protocatechuic acid + O2
5-fluoro-3-carboxy-cis,cis-muconate
-
at 2.1% the rate of protocatechuic acid oxidation
-
?
6-chloro-protocatechuate + O2
6-chloro-3-carboxy-cis,cis-muconate
-
at 4.3% the rate of protocatechuic acid oxidation
-
?
catechin + O2
?
-
-
-
-
?
catechol + O2
cis,cis-muconate
protocatechuate + O2
3-carboxy-cis,cis-muconate
protocatechuate + O2
beta-carboxy-cis-cis-muconate
protocatechuic acid + O2
3-carboxy-cis,cis-muconic acid
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
additional information
?
-
2,3-dihydroxybenzoate + O2
?
23.6% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,3-dihydroxybenzoate + O2
?
23.6% of the activity with protocatechuate for the free enzyme, 149.3% for the calcium alginate-immobilized enzyme, and 119.8% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,4-dihydroxybenzoate + O2
?
43.5% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + O2
?
43.5% of the activity with protocatechuate for the free enzyme, 96.5% for the calcium alginate-immobilized enzyme, and 65.6% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,5-dihydroxybenzoate + O2
?
33.46% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + O2
?
33.5% of the activity with protocatechuate for the free enzyme, 158.6% for the calcium alginate-immobilized enzyme, and 72.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,6-dihydroxybenzoate + O2
?
30.5% of the activity with protocatechuate for the free enzyme, 90.4% for the calcium alginate-immobilized enzyme, and 36.2% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,6-dihydroxybenzoate + O2
?
30.51% activity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
absolute requirement for vicinal hydroxyl groups in the 3- and 4-position
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 2-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-bromo-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
methylene blue cannot replace O2 as electron acceptor
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
Nocardia erythropolis
-
enzyme is active on a wide range of o-dihydroxyphenyl compounds
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with: 3,4-dihydroxyphenylacetic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 3,4-dihydroxymandelic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 4'-methylcatechol
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with: 3,4-dihydroxyphenylacetic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 3,4-dihydroxymandelic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 4'-methylcatechol
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
i.e. protocatechuate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
specific for protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
best substrate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
best substrate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
?
3,4-dihydroxybenzoate + O2
?
-
spectroscopic and electronic structure study of the enzyme-substrate complex
-
-
?
3,4-dihydroxybenzoate + O2
?
-
spectroscopic and electronic structure study of the enzyme-substrate complex
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxymandelic acid + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3,4-dihydroxymandelic acid + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3,4-dihydroxymandelic acid + O2
?
Nocardia erythropolis
-
at 5.4% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 13% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
-
-
-
?
3,5-dihydroxybenzoate + O2
?
44.3% of the activity with protocatechuate for the free enzyme, 113.3% for the calcium alginate-immobilized enzyme, and 42.9% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,5-dihydroxybenzoate + O2
?
44.33% activity compared to 3,4-dihydroxybenzoate
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 5% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
Nocardia erythropolis
-
at 14.4% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
?
4-hydroxybenzoic acid + O2
?
-
-
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
Nocardia erythropolis
-
at 3.1% the rate of protocatechuic acid oxidation
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxygenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxygenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxygenase type II only
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
caffeic acid + O2
?
34.21% activity compared to 3,4-dihydroxybenzoate
-
-
?
caffeic acid + O2
?
34.21% activity compared to 3,4-dihydroxybenzoate
-
-
?
caffeic acid + O2
?
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
catechol + O2
cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2
cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
-
at 3% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
Nocardia erythropolis
-
at 33.8% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
protocatechuate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
protocatechuate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
pyrogallol + O2
?
-
at 10% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
Nocardia erythropolis
-
at 36% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 35% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
-
-
-
-
?
vanillic acid + O2
?
-
-
-
?
vanillic acid + O2
?
-
-
-
?
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
?
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
?
additional information
?
-
-
no activity with gentisate
-
-
?
additional information
?
-
-
enzyme involved in last ring fission in naphtalene degradation, intermediates confirm proceeding through protocatechuic acid via ortho-claevage pathway
-
-
?
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
?
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
?
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
?
additional information
?
-
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
?
additional information
?
-
-
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
?
additional information
?
-
-
strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
?
additional information
?
-
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
-
-
?
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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
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
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.
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
-
greatly reduced rate of protocatechuate oxygenation
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
-
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-
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Protocatechuate 3, 4-dioxygenase from Acinetobacter calcoaceticus
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Protocatechuate 3,4-dioxygenase from Nocardia erythropolis
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Nocardia erythropolis
-
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Pseudomonas putida
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Purification and characterization of a novel type of protocatechuate 3,4-dioxygenase with the ability to oxidize 4-sulfocatechol
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1996
Agrobacterium tumefaciens, Hydrogenophaga palleronii, Agrobacterium tumefaciens S2, Hydrogenophaga palleronii S1
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Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding
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10052-10066
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Pseudomonas putida
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Cyanide and nitric oxide binding to reduced protocatechuate 3,4-dioxygenase: insight into the basis for order-dependent ligand binding by intradiol catecholic dioxygenases
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Pseudomonas putida
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The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates
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2131-2144
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no activity in Pseudomonas fluorescens, Pseudomonas putida
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Key aromatic-ring-cleaving enzyme, protocatechuate 3,4-dioxygenase, in the ecologically important marine Roseobacter lineage
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Roseobacter sp., Sagittula stellata
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Burkholderia cepacia
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Pseudomonas putida
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Pseudomonas putida
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Pseudomonas putida
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Corynebacterium glutamicum
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Geobacillus sp.
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Geobacillus sp.
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The effects of trace elements, cations, and environmental conditions on protocatechuate 3,4-dioxygenase activity
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Stenotrophomonas maltophilia, Stenotrophomonas maltophilia KB2
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