Information on EC 3.5.99.5 - 2-aminomuconate deaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.99.5
-
RECOMMENDED NAME
GeneOntology No.
2-aminomuconate deaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH3
show the reaction diagram
Intermediate in the biodegradation of nitrobenzene by Pseudomonas pseudocaligenes JS45. The reaction is spontaneous in acid conditions
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-amino-3-carboxymuconate semialdehyde degradation to 2-oxopentenoate
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2-amino-3-carboxymuconate semialdehyde degradation to glutaryl-CoA
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2-aminophenol degradation
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4-nitrotoluene degradation II
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Tryptophan metabolism
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tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-aminomuconate aminohydrolase
2-Aminomuconate is an intermediate in the bacterial biodegradation of nitrobenzene. The enzyme has been isolated from several species, including Pseudomonas pseudocaligenes JS45, Pseudomonas fluorescens KU-7, Pseudomonas sp. AP3 and Burkholderia cenocepacia J2315. The reaction is spontaneous in acid conditions.
CAS REGISTRY NUMBER
COMMENTARY hide
201098-29-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain J2315
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-
Manually annotated by BRENDA team
strain J2315
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-
Manually annotated by BRENDA team
strain HS12
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-
Manually annotated by BRENDA team
strain HS12
-
-
Manually annotated by BRENDA team
strain Ap-3
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-
Manually annotated by BRENDA team
strain Ap-3
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminomuconate + H2O
4-oxalocrotonate + NH3
show the reaction diagram
2-aminomuconate + H2O
?
show the reaction diagram
additional information
?
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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
2-aminomuconate + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
slightly inhibits
CuSO4
-
2 mM, 20% inhibition
diethyldicarbonate
-
2 mM, complete inhibition
Hg2+
-
slightly inhibits
MnCl2
-
2 mM, 20% inhibition
Pb2+
-
slightly inhibits
phenylhydrazine
-
10 mM, 20% inhibition
ZnCl2
-
2 mM, 70% inhibition
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
2-aminomuconate
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
208
2-aminomuconate
Pseudomonas pseudoalcaligenes
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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4 * 16000, SDS-PAGE
16600
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6 * 16600, SDS-PAGE
18000
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overexpressed soluble protein
67000
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gel filtration
100000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homotetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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-
667336
5.7 - 8.8
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at room temperature for at least 3 h
172186
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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stable for at least 3 days
60
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77% loss of activity in 5 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel-nitrilotriacetic acid affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into plasmid pBR328, expression in Escherichia coli JM109 harboring plasmids pHS29, pHS293, pHS295, pHS291, pHS2915 and PHS2916
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cloned into plasmid pDESTF1 and overexpressed in Escherichia coli Tuner (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
molecular biology
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