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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
2-hydroxychromene-2-carboxylate isomerase, 2hc2ca isomerase,
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2-hydroxychromene-2-carboxylate isomerase
2-hydroxychromene-2-carboxylic acid isomerase
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2-hydroxychromene-2-carboxylate isomerase
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2-hydroxychromene-2-carboxylate isomerase
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2-hydroxychromene-2-carboxylate isomerase
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2HC2CA isomerase
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2HCCAI
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nsaD
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2-hydroxy-2H-chromene-2-carboxylate = (3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
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2-hydroxy-2H-chromene-2-carboxylate-(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate isomerase
This enzyme is involved in naphthalene degradation.
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
2-hydroxybenzo[g]chromene-2-carboxylate
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additional information
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
extracts of Escherichia coli JM109 carrying pRE718 catalyze the conversion of trans-o-hydroxybenzylidenepyruvate or 2-hydroxychromene-2-carboxylate to an equilibrium mixture that contained 55% 2-hydroxychromene-2-carboxylate and 45% trans-o-hydroxybenzylidenepyruvate at pH 7. At pH 10 the reaction occus entirely in on direction, the conversion of 2-hydroxychromene-2-carboxylate to trans-o-hydroxybenzylidenepyruvate. The product is identified by nuclear magnetic resonance spectroscopy. This isomerization occurs spontaneously, although at a slower rate than the enzyme-catalyzed reaction
i.e. (E)-2'-hydroxybenzylidenepyruvate, i.e. trans-o-hydroxybenzylidenepyruvate
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
glutathione (GSH)-dependent interconversion. The isomerization reaction involves a short-lived covalent adduct between the sulfur of GSH and C7 of the substrate
i.e. (E)-2'-hydroxybenzylidenepyruvate, i.e. trans-o-hydroxybenzylidenepyruvate
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
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the product trans-o-hydroxybenzylidenepyruvate is analyzed by 1H NMR spectrum
i.e. (E)-2'-hydroxybenzylidenepyruvate, i.e. trans-o-hydroxybenzylidenepyruvate
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2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
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the product trans-o-hydroxybenzylidenepyruvate is analyzed by 1H NMR spectrum
i.e. (E)-2'-hydroxybenzylidenepyruvate, i.e. trans-o-hydroxybenzylidenepyruvate
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2-hydroxybenzo[g]chromene-2-carboxylate
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more unstable than 2-hydroxychromene-2-carboxylate
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2-hydroxybenzo[g]chromene-2-carboxylate
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more unstable than 2-hydroxychromene-2-carboxylate
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additional information
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enzyme degrades naphthalenesulfonates
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additional information
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2,5-dihydroxychromene-2-carboxylate is no substrate
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additional information
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enzyme degrades naphthalenesulfonates
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additional information
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2,5-dihydroxychromene-2-carboxylate is no substrate
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additional information
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additional information
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enzyme degrades naphthalenesulfonates
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additional information
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enzyme degrades naphthalenesulfonates
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glutathione
the dimeric protein binds one molecule of GSH very tightly and a second molecule of GSH with much lower affinity. The enzyme is unstable in the absence of GSH. The turnover number in the forward direction greatly exceeds off rates for GSH, suggesting that GSH acts as a tightly bound cofactor in the reaction. Km: 0.017 mM
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additional information
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no increase of enzyme activity is found after (pre)incubation of the enzyme with ZnSO4, COCl2, FeCl2 or MnCl2 (each 2 mM)
additional information
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no increase of enzyme activity is found after (pre)incubation of the enzyme with ZnSO4, COCl2, FeCl2 or MnCl2 (each 2 mM)
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(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
i.e. (E)-2'-hydroxybenzylidenepyruvate
additional information
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no significant inhibition is observed after one day incubation with 50 mM EDTA
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additional information
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no significant inhibition is observed after one day incubation with 50 mM EDTA
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glutathione
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no enzyme activity is found when the enzyme preparations have been preincubated without or with only 10 mM glutathione
glutathione
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highest enzyme activity is found after preincubation of the enzyme with glutathione at alkaline pH-values. To determine enzyme activities during the purification procedure, it is necessary to reactivate the enzyme with glutathione
glutathione
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activates above 0.15 mM
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0.138
(E)-2'-hydroxybenzylidenepyruvate
pH 7.0, 25°C
0.053 - 0.27
2-hydroxy-2H-chromene-2-carboxylate
0.084 - 0.23
2-hydroxychromene-2-carboxylate
0.053
2-hydroxy-2H-chromene-2-carboxylate
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pH 7.4, 30°C
0.27
2-hydroxy-2H-chromene-2-carboxylate
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0.084
2-hydroxychromene-2-carboxylate
pH 7.0, 25°C
0.23
2-hydroxychromene-2-carboxylate
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19
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
pH 7.0, 25°C
47
2-hydroxy-2H-chromene-2-carboxylate
pH 7.0, 25°C
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0.136
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
pH 7.0, 25°C
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0.14
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for 2-hydroxychromene-2-carboxylate as substrate
0.27
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for 2-hydroxychromene-2-carboxylate as substrate
55.4
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last purification step
0.005
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spectrophotometrically
0.005
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spectrophotometrically
0.2
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enzyme activity increases when the cell extract is incubated for 15 min with glutathione (5 mM) prior to the assay. The addition of glutathione (0.2 mM) directly to the assay does not increase enzyme activity
0.2
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enzyme activity increases when the cell extract is incubated for 15 min with glutathione (5 mM) prior to the assay. The addition of glutathione (0.2 mM) directly to the assay does not increase enzyme activity
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9
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in glycine-NaOH-buffer, highest enzyme activity is found after preincubation of the enzyme with glutathione at alkaline pH-values
9.5
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in glycine-NaOH-buffer
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8 - 9.3
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effect of glutathione is optimal between pH 8 and pH 9.3. In contrast, no activation is observed when the enzyme is incubated with glutathione at pH 5.0. Activities higher than 70% of this optimal activity are found at pH-values in the range 8.0-9.5 in glycine-NaOH- or Tris/HC1-buffer. At pH 7 about 50% and at pH 5.5 10% of the optimal activity is observed
8 - 9.5
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at pH 9.0 50% and at pH 8.0 only 5% of the maximal activity is found, respectively
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6.8 - 9.5
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pH 6.8: about 35% of maximal activity, pH 9.5: about 40% of maximal activity
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5.4
calculated from sequence
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BN6, DSM 6383
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brenda
A3, DSM 676
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brenda
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SwissProt
brenda
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brenda
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brenda
BN6
SwissProt
brenda
BN6
SwissProt
brenda
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23031
x * 23031, calculated from sequence
25000
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1 * 25000, SDS-PAGE
24700
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SDS-PAGE
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x * 23031, calculated from sequence
monomer
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1 * 24700, SDS-PAGE
monomer
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1 * 24700, SDS-PAGE
monomer
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1 * 25000, SDS-PAGE
monomer
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1 * 25000, SDS-PAGE
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crystal structure of the enzyme at 1.7 A resolution
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1.5 - 10
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4°C, 40 h, stable in the range of pH 1.5 to 10.0
698643
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45
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10 min, stable at temperature up to
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10 min, in presence of glutathione at 2.5 mM, the enzyme is stable up to
55
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10 min, 13% of the original activity remains. In presence of glutathione at 2.5 mM, 68% of the original activity remains after 10 min
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unstable in absence of GSH
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4C, purifed enzyme, Tris HCl, pH 7.5, 100 mM NaCl, 1 month 52% loss of activity
4C, purifed enzyme, Tris HCl, pH 7.5, 100 mM NaCl, 1 month 52% loss of activity
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4C, purifed enzyme, Tris HCl, pH 7.5, 100 mM NaCl, 1 month 52% loss of activity
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at room temperature by use of a fast-protein liquid chromatography system
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partially purified by anion-exchange chromatography
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a gene cluster is identified on the plasmid pBN6 which codes for several enzymes participating in the degradative pathway for naphthalenesulfonates. A DNA fragment of 16915 bp is sequenced which contains 17 ORFs. The genes encoding the 1,2-dihydroxynaphthalene dioxygenase, 2-hydroxychromene-2-carboxylate isomerase, and 29-hydroxybenzalpyruvate aldolase of the naphthalenesulfonate pathway are identified on the DNA fragment and the encoded proteins are heterologously expressed in Escherichia coli
expression in Escherichia coli
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Eaton, R.W.; Chapman, P.J.
Bacterial metabolism of naphthalene: Construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions
J. Bacteriol.
174
7542-7554
1992
Pseudomonas putida (Q51948)
brenda
Thompson, L.C.; Ladner, J.E.; Codreanu, S.G.; Harp, J.; Gilliland, G.L.; Armstrong, R.N.
2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida
Biochemistry
46
6710-6722
2007
Pseudomonas putida (Q51948)
brenda
R. W., Eaton
Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid
J. Bacteriol.
176
7757-7762
1994
Pseudomonas putida (Q51948)
brenda
Ohmoto, T.; Kinoshita, T.; Moriyoshi, K.; Sakai, K.; Hamada, N.; Ohe, T.
Purification and some properties of 2-hydroxychromene-2-carboxylate isomerase from naphthalenesulfonate-assimilating Pseudomonas sp. TA-2
J. Biochem.
124
591-597
1998
Pseudomonas sp., Pseudomonas sp. TA-2
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Keck, A.; Conradt, D.; Mahler, A.; Stolz, A.; Mattes, R.; Klein, J.
Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6
Microbiology
152
1929-1940
2006
Sphingobium xenophagum (Q9X9Q7), Sphingobium xenophagum, Sphingobium xenophagum BN6 (Q9X9Q7)
brenda
Kuhm, A.E.; Knackmuss, H.-J.; Stolz, A.
2-Hydroxychromene-2-carboxylate isomerase from bacteria that degrade naphthalenesulfonates
Biodegradation
4
155-162
1993
Brevundimonas vesicularis, Comamonas testosteroni
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brenda
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