Information on EC 4.2.1.49 - Urocanate hydratase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.1.49
-
RECOMMENDED NAME
GeneOntology No.
Urocanate hydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Histidine metabolism
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L-histidine degradation I
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-
L-histidine degradation II
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L-histidine degradation III
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L-histidine degradation VI
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Metabolic pathways
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histidine metabolism
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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 hide
9014-58-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SH-11 derived from SB 19
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
N.C.I.B. 10808
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Manually annotated by BRENDA team
N.C.I.B. 10808
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
ATCC 11299b
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Manually annotated by BRENDA team
white clover
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Aminourocanate + H2O
2-Aminoimidazolone propionate
show the reaction diagram
-
reacts 1000 times more slowly than urocanate
-
-
-
2-Fluorourocanate + H2O
2-Fluoroimidazolone propionate
show the reaction diagram
2-Methylurocanate + H2O
2-Methylimidazolone propionate
show the reaction diagram
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate
urocanate + H2O
show the reaction diagram
Urocanate + H2O
4,5-Dihydro-4-oxo-5-imidazolepropanoate
show the reaction diagram
Urocanate + H2O
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate
urocanate + H2O
show the reaction diagram
Urocanate + H2O
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Fluorourocanate
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competitive
2-mercaptoethanol
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2-Methylimidazolone propionate
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2-Methylurocanate
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3-Mercaptopropionate
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4-bromocrotonate
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irreversible inhibition
crotonate
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cyanide
dithioerythritol
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glycylglycine
hydroxylamine
Imidazolepropionate
Imidazolepyruvate
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non-competitive
imidazolone propionate
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-
NaBH4
O-Methylhydroxylamine
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p-Chloromercuriphenylsulfonate
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p-mercuribenzoate
phenylhydrazine
Semicarbazide
Sodium dithionite
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succinate
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competitive
Sulfide
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sulfite
thioglycolate
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competitive
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
2-Fluorourocanate
-
-
0.005 - 0.7
Urocanate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003
Cu2+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.131
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-
1.6
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 50
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30% of maximal activity at 0C, no activity about 50C
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
2 * 54000 sedimentation equilibrium centrifugation
60000
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2 * 60000, SDS-PAGE
61401
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2 * 61401, calculation from amino acid sequence
61404
x * 61404, calculated from amino acid sequence
110000
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sedimentation equilibrium centrifugation
118000
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meniscus depletion method
120000
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sucrose density gradient centrifugation
122000
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gel filtration of the over-expressed enzyme
127000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61404, calculated from amino acid sequence
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
5 min, 60% loss of activity
60
-
5 min, 80% loss of activity
70
-
5 min, 100% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable enzyme, pyridoxal 5'-phosphate partially stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for many months
-
-16C, lyophilized, stable for several weeks
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-18C, 0.1 M phosphate buffer, pH 7.0, stable for many weeks
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-20C, 40% loss of activity after 3 months
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addition of glycerol to a final concentration of 50% prevents inactivation of the enzyme at 4C
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presence of 0.01 M 2-mercaptoethanol in the buffer results in total inactivation of the enzyme upon freezing
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and mutant enzymes, by sonication, centrifugation and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
genomic clone, overexpressed in Escherichia coli
UROC1 gene cloned into the expression vector pET100/D-TOPO with an N-terminal tag containing the Xpress epitope and a 6xHis-tag. Expressed in Escherichia coli BL21Start (D3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
urocanase activity is 14fold higher in cells grown at 4C than at 20C
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L70P/R450C
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L70P and R450C mutations in the coding region of the UROC1 gene in a girl with urocanic aciduria presenting with mental retardation and intermittent ataxia. Both mutations cannot produce a fully functional enzyme, L70P substitution implies the disruption of an alpha-helix in the N-terminus, which alters its properties and therefore, its function. The R450C change renders impossible any interaction between urocanase and its substrate and loses its enzyme activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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L70P and R450C mutations in the coding region of the UROC1 gene in a girl with urocanic aciduria presenting with mental retardation and intermittent ataxia. Both mutations cannot produce a fully functional enzyme, L70P substitution implies the disruption of an alpha-helix in the N-terminus, which alters its properties and therefore, its function. The R450C change renders impossible any interaction between urocanase and its substrate and loses its enzyme activity
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