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Information on EC 3.5.99.5 - 2-aminomuconate deaminase
for references in articles please use BRENDA:EC3.5.99.5
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.99 In other compounds
3.5.99.5 2-aminomuconate deaminase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
- 3.5.99.5
- 2-aminophenol
- 4-oxalocrotonate
- ammonia
- nitrobenzene
- hydroxylaminobenzene
- 6-semialdehyde
-
meta-cleavage
- pseudoalcaligenes
-
deamination
-
1,6-dioxygenase
- acetaldehyde
- molecular biology
- degradation
showSynonyms
2-aminomuconate deaminase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-AM deaminase
2-aminomuconate deaminase
AMD
amnD
deaminase, 2-aminomuconate
-
-
-
-
nbzE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate + NH3
Intermediate in the biodegradation of nitrobenzene by Pseudomonas pseudocaligenes JS45. The reaction is spontaneous in acid conditions
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-N bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
2-amino-3-carboxymuconate semialdehyde degradation to 2-hydroxypentadienoate, 2-amino-3-carboxymuconate semialdehyde degradation to glutaryl-CoA, 2-aminophenol degradation, 4-nitrotoluene degradation II
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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.
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CAS REGISTRY NUMBER
COMMENTARY
201098-29-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminomuconate + H2O
(3E)-2-oxohex-3-enedioate + NH3
Substrates: -
Products: -
Products: -
?
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: -
Products: -
Products: -
?
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: -
Products: -
Products: -
?
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: -
Products: -
Products: -
ir
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: -
Products: -
Products: -
ir
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: part of the nitrobenzene degradation pathway
Products: -
Products: -
?
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: part of the nitrobenzene degradation pathway
Products: -
Products: -
?
2-aminomuconate + H2O
4-oxalocrotonate + NH3
-
Substrates: -
Products: -
Products: -
?
2-aminomuconate + H2O
?
-
Substrates: intermediate in biodegradation of nitrobenzene
Products: -
Products: -
?
2-aminomuconate + H2O
?
-
Substrates: intermediate in biodegradation of nitrobenzene
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-aminomuconic semialdehyde, glycine, alanine, aspartic acid, glutaric acid, 2-aminoadipic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-aminomuconic semialdehyde, glycine, alanine, aspartic acid, glutaric acid, 2-aminoadipic acid
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminomuconate + H2O
?
-
Substrates: intermediate in biodegradation of nitrobenzene
Products: -
Products: -
?
2-aminomuconate + H2O
?
-
Substrates: intermediate in biodegradation of nitrobenzene
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by 2-aminomuconic semialdehyde, glycine, alanine, aspartic acid, glutaric acid, 2-aminoadipic acid
-
additional information
-
metal chelating, sulfhydryl, and surface-active agents do not affect the enzyme reaction
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homohexamer
the AmnE hexamer is in a stable state in solution, and that the residues Arg56 and Met96 located on the hexameric interface are two key residues required to maintain the hexameric conformation of AmnE
homotetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method at 20°C, crystal structure is determined at 1.75 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R56A
the mutant loses the ability to maintain the hexameric conformation, and reveales that the hydrogen bonds between residues Arg56 and Met96 have pivotal roles in the AmnE hexameric assembly
additional information
additional information
-
spontaneous mutants HS121(pNB2) during serial transfer on nonselective agar plates, can not grow on nitrobenzene as the sole source of carbon, nitrogen and energy, have lost plasmid pNB1, plasmid-cured HS124 mutant, obtained by incubating the parent strain at an elevated temperature, have lost plasmid pNB2 and also can not grow on nitrobenzene
additional information
-
spontaneous mutants HS121(pNB2) during serial transfer on nonselective agar plates, can not grow on nitrobenzene as the sole source of carbon, nitrogen and energy, have lost plasmid pNB1, plasmid-cured HS124 mutant, obtained by incubating the parent strain at an elevated temperature, have lost plasmid pNB2 and also can not grow on nitrobenzene
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
-
cloned into plasmid pDESTF1 and overexpressed in Escherichia coli Tuner (DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
molecular biology
degradation
-
new tryptophan catabolic pathway in Burholderia cepacia J2315, formation of the intermediate 4-oxalocrotonate differentiates this pathway from the proposed mammalian pathway which converts 2-aminomuconate to 2-ketoadipate and, ultimately, glutaryl-coenzyme A
degradation
-
new tryptophan catabolic pathway in Burholderia cepacia J2315, formation of the intermediate 4-oxalocrotonate differentiates this pathway from the proposed mammalian pathway which converts 2-aminomuconate to 2-ketoadipate and, ultimately, glutaryl-coenzyme A
-
molecular biology
-
nbzE, involved in the ring cleavage pathway of 2-aminophenol, is localized on the 6.6 kb SnaBI-SmaI fragment of the plasmid pNB1 and clusters in the order nbzC-nbzD-nbzE as an operon
molecular biology
-
nbzE, involved in the ring cleavage pathway of 2-aminophenol, is localized on the 6.6 kb SnaBI-SmaI fragment of the plasmid pNB1 and clusters in the order nbzC-nbzD-nbzE as an operon
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
He, Z.; Spain, J.C.
A novel 2-aminomuconate deaminase in the nitrobenzene degradation pathway of Pseudomonas pseudoalcaligenes JS45
J. Bacteriol.
180
2502-2506
1998
Ectopseudomonas oleovorans, Ectopseudomonas oleovorans JS45
brenda
He, Z.; Spain, J.C.
Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2-aminomuconic semialdehyde
Appl. Environ. Microbiol.
63
4839-4843
1997
Ectopseudomonas oleovorans, Ectopseudomonas oleovorans JS45
brenda
Takenaka, S.; Murakami, S.; Kim, Y.J.; Aoki, K.
Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3
Arch. Microbiol.
174
265-272
2000
Pseudomonas sp., Pseudomonas sp. Ap-3
brenda
Park, H.S.; Kim, H.S.
Identification and characterization of the nitrobenzene catabolic plasmids pNB1 and pNB2 in Pseudomonas putida HS12
J. Bacteriol.
182
573-580
2000
Pseudomonas putida, Pseudomonas putida HS12
brenda
Colabroy, K.L.; Begley, T.P.
Tryptophan catabolism: Identification and characterization of a new degradative pathway
J. Bacteriol.
187
7866-7869
2005
Burkholderia cepacia, Burkholderia cepacia J2315
brenda
Chen, Y.; Chen, Y.; Jiang, H.; Lu, D.; Hu, T.; Bi, G.; Ran, Y.; Yu, B.; Dong, H.; Su, D.
A unique homo-hexameric structure of 2-aminomuconate deaminase in the bacterium Pseudomonas species AP-3
Front. Microbiol.
10
2079
2019
Pseudomonas sp. AP3 (Q9KWS2)
brenda
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