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Information on EC 4.1.1.45 - aminocarboxymuconate-semialdehyde decarboxylase

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.45 aminocarboxymuconate-semialdehyde decarboxylase
IUBMB Comments
Product rearranges non-enzymically to picolinate.
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This record set is specific for:
UNIPROT: Q83V25
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acmsd, aminocarboxymuconate-semialdehyde decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, picolinic carboxylase, acmsdase, hacmsd, 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase, acmsd i, acms decarboxylase, alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
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alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
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3-(3-oxoprop-2-enyl)-2-aminobut-2-endioate carboxy-lyase
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-
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ACMSD
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-
-
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alpha-Amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase
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-
-
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alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde beta-decarboxylase
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-
-
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Amino-carboxymuconate-semialdehyde decarboxylase
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-
-
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Decarboxylase, aminocarboxymuconate semialdehyde
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-
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Picolinic acid carboxylase
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-
-
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Picolinic acid decarboxylase
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-
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Picolinic decarboxylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming)
Product rearranges non-enzymically to picolinate.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-47-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate
2-aminomuconate-6-semialdehyde + CO2
show the reaction diagram
2-nitrobenzoate degradation pathway
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
Q83V25_PSEFL
334
0
37141
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37140
deduced from DNA sequence
38700
recombinant protein, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzymes Co(II)-H228Y, Zn(II)-H228Y, and Zn(II)-H228G, hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.75), 0.2 M MgCl2, and 15% (w/v) PEG 5000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H228G
the mutant contains iron rather than zinc and is catalytically inactive
H228Y
the mutant contains iron rather than zinc and is catalytically inactive
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
nbaD gene overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Muraki, T.; Taki, M.; Hasegawa, Y.; Iwaki, H.; Lau, P.C.
Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7
Appl. Environ. Microbiol.
69
1564-1572
2003
Pseudomonas fluorescens (Q83V25), Pseudomonas fluorescens, Pseudomonas fluorescens KU-7 (Q83V25)
Manually annotated by BRENDA team
Huo, L.; Fielding, A.J.; Chen, Y.; Li, T.; Iwaki, H.; Hosler, J.P.; Chen, L.; Hasegawa, Y.; Que, L.; Liu, A.
Evidence for a dual role of an active site histidine in alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase
Biochemistry
51
5811-5821
2012
Pseudomonas fluorescens (Q83V25), Pseudomonas fluorescens
Manually annotated by BRENDA team