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Information on EC 4.2.1.49 - urocanate hydratase and Organism(s) Pseudomonas putida and UniProt Accession P25080
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4.2.1.49 urocanate hydrataseIUBMB Comments
Contains tightly bound NAD+.
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Word Map
- 4.2.1.49
- putida
- histidase
- photoactivation
- l-histidine
-
histidine-pyruvate
- formiminoglutamate
- medicine
The taxonomic range for the selected organisms is: Pseudomonas putida
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
urocanase, urocanate hydratase, uroc1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4'-Imidazolone-5'-propionate hydro-lyase
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4,5-dihydro-4-oxo-5-imidazole-propanoate hydro-lyase
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4-Imidazolone-5'-propionate hydrolyase
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Hydratase, urocanate
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Imidazolonepropionate hydrolase
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Urocanase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
investigation of a regulation mechanism not dependent on light
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3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
identification of the enol tautomer of imidazolone propionate as the reaction product
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3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
investigation of the mechanism and stereospecificity by using 1H-NMR and C-NMR spectroscopy #1,2,4-8,12-14#
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3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
catalytic and thermodynamic properties of the reaction
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3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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SYSTEMATIC NAME
IUBMB Comments
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate hydro-lyase (urocanate-forming)
Contains tightly bound NAD+.
CAS REGISTRY NUMBER
COMMENTARY
9014-58-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Aminourocanate + H2O
2-Aminoimidazolone propionate
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reacts 1000 times more slowly than urocanate
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-
?
2-Fluorourocanate + H2O
2-Fluoroimidazolone propionate
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reacts 150 times more slowly than urocanate
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-
?
2-Methylurocanate + H2O
2-Methylimidazolone propionate
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reacts 128 times more slowly than urocanate
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?
Urocanate + H2O
4,5-Dihydro-4-oxo-5-imidazolepropanoate
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highly specific
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
sulfite-treated inactive enzyme is photoactivatable
additional information
-
sulfite-treated inactive enzyme is photoactivatable
additional information
-
NaBH4 treated inactive enzyme is partially photoactivatable
additional information
-
NaBH4 treated inactive enzyme is partially photoactivatable
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Km value is not drastically altered over the temperature range of 20¦C to 40¦C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, crystallized after removing one of the seven free thiol groups. The crystal structure is solved by multiwavelength anomalous diffraction using a seleno-methionine derivative and then refined at 1.14 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
George, D.J.; Phillips, A.T.
Identification of alpha-ketobutyrate as the prosthetic group of urocanase from Pseudomonas putida
J. Biol. Chem.
245
528-537
1970
Gallus gallus, Felis catus, Pseudomonas putida
Kaeppeli, F.; Retey, J.
Studies on the mechanism and stereospecificity of the urocanase reaction
Eur. J. Biochem.
23
198-202
1971
Bos taurus, Pseudomonas putida
Phillips, A.T.; George, D.J.
Urocanase (Pseudomonas putida)
Methods Enzymol.
17B
73-79
1971
Bos taurus, Felis catus, Pseudomonas putida
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Lynch, M.C.; Phillips, A.T.
Urocanase of Pseudomonas putida
J. Biol. Chem.
247
7799-7805
1972
Pseudomonas putida
Hug, D.H.; Roth, D.
Inhibition of urocanase by cupric ion
Biochim. Biophys. Acta
293
497-505
1973
Pseudomonas putida, Pseudomonas putida A3.12
Hug, D.H.; Hunter, J.K.
Effect of temperature on urocanase from a psychrophile, Pseudomonas putida
Biochemistry
13
1427-1430
1974
Pseudomonas putida, Pseudomonas putida A3.12, Rattus norvegicus
Cohn, M.S.; Lynch, M.C.; Phillips, A.T.
Catalytic and thermodynamic properties of the urocanate hydratase reaction
Biochim. Biophys. Acta
377
444-453
1975
Pseudomonas putida
Lane R.S.; Scheuer, S.A.; Thill, G.; Dyll, R.J.
Irreversible inactivation of urocanase by 4-bromocrotonate
Biochem. Biophys. Res. Commun.
71
400-407
1976
Pseudomonas putida
Egan, R.M.; Phillips, A.T.
Presence of tightly bound NAD+ in urocanase of Pseudomonas putida
J. Biol. Chem.
252
5701-5707
1977
Pseudomonas putida, Pseudomonas putida A3.12
Hug, D.H.; O'Donnell, P.S.; Hunter, J.K.
Photoactivation of urocanase in Pseudomonas putida
J. Biol. Chem.
253
7622-7629
1978
Pseudomonas putida, Pseudomonas putida A3.12
Hug, D.H.; O'Donnell, P.S.; Hunter, J.K.
Thioglycolate, competitive inhibitor of urocanase
Biochem. Biophys. Res. Commun.
81
1435-1442
1978
Pseudomonas putida, Pseudomonas putida A3.12
Keul, V.; Kaeppeli, F.; Ghosh, C.; Krebs, T.; Robinson, J.A.; Retey, J.
Identification of the prosthetic group of urocanase
J. Biol. Chem.
254
843-851
1979
Bos taurus, Pseudomonas putida
O'Donnell, P.S.; Hug, D.H.; Hunter, J.K.
Sulfhydryl groups in urocanase: Relationship to nicotinamide adenine dinucleotide binding
Arch. Biochem. Biophys.
202
242-249
1980
Pseudomonas putida, Pseudomonas putida A3.12
Gerlinger, E.; Hull, W.E.; Retey, J.
Mechanistic study of urocanase reaction using deuterated substrates and 1H-NMR spectroscopy
Eur. J. Biochem.
117
629-634
1981
Pseudomonas putida
Hug, D.H.; Hunter, J.K.
Roles of cysteine sulfinate and transaminase on in vivo dark reversion of urocanase in Pseudomonas putida
J. Bacteriol.
151
813-818
1982
Pseudomonas putida, Pseudomonas putida A3.12
Matherly, L.H.; Phillips, A.T.
Identification of enol tautomer of imidazolone propionate as the urocanase reaction product
Arch. Biochem. Biophys.
220
314-317
1983
Pseudomonas putida
Gerlinger, E.; Hull, W.E.; Retey, J.
Mechanistic studies of the urocanase reaction using 1H- and 31P-NMR spectroscopy and the substrate analogue 2-methylurocanate
Tetrahedron
39
3523-3528
1983
Pseudomonas putida
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Hug, D.H.; O'Donnell, P.S.
Evidence against a temperature-dependent conformational change in urocanase from Pseudomonas putida
Biochim. Biophys. Acta
830
101-104
1985
Pseudomonas putida, Pseudomonas putida A3.12
Consevage, M.W.; Porter, R.D.; Phillips, A.T.
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida
Venema, R.C.; Hug, D.H.
Activation of urocanase from Pseudomonas putida by electronically excited triplet species
J. Biol. Chem.
260
12190-12193
1985
Pseudomonas putida, Pseudomonas putida A3.12
Gerlinger, E.; Retey, J.
Proposal for the mechanism of action of urocanase. Interference from the inhibition by 2-methylurocanate
Z. Naturforsch. C
42
349-352
1987
Pseudomonas putida
O'Donnell, P.S.; Hug, D.H.
Thermal activation of photoactivatable urocanase from Pseudomonas putida
J. Photochem. Photobiol. B, Biol.
3
429-435
1989
Pseudomonas putida, Pseudomonas putida A3.12
Hunter, J.K.; Hug, D.H.
Specific inhibition of bacterial and bovine urocanase by glycylglycine
Pept. Res.
2
240-245
1989
Bos taurus, Pseudomonas putida, Pseudomonas putida A3.12
Klepp, J.; Fallert-Mller, A.; Grimm, K.; Hull, W.E.; Retey, J.
Mechanism of action of urocanase
Eur. J. Biochem.
192
669-676
1990
Pseudomonas putida
Klepp, J.; Retey, J.
The stoichiometry of the tightly bound NAD+ in urocanase
Eur. J. Biochem.
185
615-619
1989
Pseudomonas putida
Lenz, M.; Retey, J.
Cloning, expression and mutational analysis of the urocanase gene (hutU) from Pseudomonas putida
Eur. J. Biochem.
217
429-434
1993
Pseudomonas putida
Retey, J.
The urocanase story: A novel role of NAD+ as electrophile
Arch. Biochem. Biophys.
314
1-16
1994
Bacillus subtilis, Bos taurus, Cavia porcellus, Clostridium tetanomorphum, Felis catus, Gallus gallus, Klebsiella aerogenes, Pseudomonas putida, Rattus norvegicus, Trifolium repens
Schubert, C.; Roettele, H.; Spraul, M.; Retey, J.
On the mechanism of action of urocanase: observation of the enzyme-bound NAD+ -inhibitor adduct by 13C NMR spectroscopy
Angew. Chem. Int. Ed. Engl.
34
652-4
1995
Pseudomonas putida
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