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Information on EC 3.5.2.18 - enamidase and Organism(s) Eubacterium barkeri and UniProt Accession Q0QLE9

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.18 enamidase
IUBMB Comments
Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Delta-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
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This record set is specific for:
Eubacterium barkeri
UNIPROT: Q0QLE9
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The taxonomic range for the selected organisms is: Eubacterium barkeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
enamidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
-
hydrolysis of C-N bond
-
-
SYSTEMATIC NAME
IUBMB Comments
6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase
Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Delta-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
CAS REGISTRY NUMBER
COMMENTARY hide
911980-63-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4,5,6-tetrahydro-6-oxonicotinate + H2O
2-(enamine)glutarate + NH3
show the reaction diagram
-
-
-
?
2-(enamine)glutarate + H2O
(S)-2-formylglutarate + NH3
show the reaction diagram
-
-
-
?
6-oxo-1,4,5,6-tetrahydronicotinate + H2O
2-formylglutarate + NH3
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
6-oxo-1,4,5,6-tetrahydronicotinate + H2O
2-formylglutarate + NH3
show the reaction diagram
-
the enzyme forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
contains 1.0 Fe per subunit. The Fe/Zn binuclear metal center of enamidase catalyzes amide hydrolysis of 6-oxo-1,4,5,6-tetrahydronicotinate, hydration and ammonia elimination
Zn
-
contains about 0.6 Zn per subunit
additional information
-
the enzyme contains the typical metal binding His-X-His pattern in the N-terminal part
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB: 2vun
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENA_EUBBA
386
0
39923
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
178000
size-exclusion chromatography
39793
-
4 * 39793, MALDI-TOF MS
40000
-
4 * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL 21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alhapel, A.; Darley, D.J.; Wagener, N.; Eckel, E.; Elsner, N.; Pierik, A.J.
Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri
Proc. Natl. Acad. Sci. USA
103
12341-12346
2006
Eubacterium barkeri
Manually annotated by BRENDA team
Kress, D.; Alhapel, A.; Pierik, A.J.; Essen, L.O.
The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism
J. Mol. Biol.
384
837-847
2008
Eubacterium barkeri (Q0QLE9), Eubacterium barkeri
Manually annotated by BRENDA team