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Information on EC 5.99.1.4 - 2-hydroxychromene-2-carboxylate isomerase and Organism(s) Pseudomonas putida and UniProt Accession Q51948

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IUBMB Comments
This enzyme is involved in naphthalene degradation.
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This record set is specific for:
Pseudomonas putida
UNIPROT: Q51948
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The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-hydroxychromene-2-carboxylate isomerase, 2hc2ca isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hydroxychromene-2-carboxylate isomerase
-
2-hydroxychromene-2-carboxylic acid isomerase
-
SYSTEMATIC NAME
IUBMB Comments
2-hydroxy-2H-chromene-2-carboxylate-(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate isomerase
This enzyme is involved in naphthalene degradation.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxy-2H-chromene-2-carboxylate
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
i.e. (E)-2'-hydroxybenzylidenepyruvate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.138
(E)-2'-hydroxybenzylidenepyruvate
pH 7.0, 25°C
0.084
2-hydroxychromene-2-carboxylate
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.136
(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate
pH 7.0, 25°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAHD_PSEPU
203
0
23061
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23031
x * 23031, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 23031, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme at 1.7 A resolution
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in absence of GSH
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team