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Literature summary extracted from

  • Alhapel, A.; Darley, D.J.; Wagener, N.; Eckel, E.; Elsner, N.; Pierik, A.J.
    Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri (2006), Proc. Natl. Acad. Sci. USA, 103, 12341-12346.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.291 expression in Escherichia coli Eubacterium barkeri
4.1.3.32 expressed in Escherichia coli BL21 cells Eubacterium barkeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.291 0.1
-
 NAD+
-
 Eubacterium barkeri
1.1.1.291 1.1
-
 2-hydroxymethylglutarate
-
 Eubacterium barkeri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.7.1 Fe2+ one (2Fe-2S)2+/1+ and two (4Fe-4S)2+/1+ clusters Eubacterium barkeri
3.5.2.18 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 Eubacterium barkeri
3.5.2.18 additional information the enzyme contains the typical metal binding His-X-His pattern in the N-terminal part Eubacterium barkeri
3.5.2.18 Zn contains about 0.6 Zn per subunit Eubacterium barkeri
4.1.3.32 Mg2+ dependent Eubacterium barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.291 32000
-
 4 * 32000, SDS-PAGE Eubacterium barkeri
1.3.7.1 53000
-
 gel filtration Eubacterium barkeri
3.5.2.18 39793
-
 4 * 39793, MALDI-TOF MS Eubacterium barkeri
3.5.2.18 40000
-
 4 * 40000, SDS-PAGE Eubacterium barkeri
4.1.3.32 31400
-
 4 * 31400, SDS-PAGE Eubacterium barkeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.291 2-formylglutarate + NADH + H+ Eubacterium barkeri the enzyme forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri 2-hydroxymethylglutarate + NAD+
-
 ?
3.5.2.18 6-oxo-1,4,5,6-tetrahydronicotinate + H2O Eubacterium barkeri the enzyme forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri 2-formylglutarate + NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.291 Eubacterium barkeri
-
-
-
1.3.7.1 Eubacterium barkeri
-
 strain DSMZ 1223
-
3.5.2.18 Eubacterium barkeri
-
-
-
4.1.3.32 Eubacterium barkeri
-
 strain DSMZ 1223
-
5.3.3.6 Eubacterium barkeri
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.1.1.291 instability under anaerobic conditions Eubacterium barkeri

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.291
-
 Eubacterium barkeri
1.3.7.1 under strictly anaerobic conditions Eubacterium barkeri
3.5.2.18
-
 Eubacterium barkeri
4.1.3.32 (NH4)2SO4 precipitation, Source Phe column chromatography, and Source 15Q FPLC column chromatography Eubacterium barkeri

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.7.1 350
-
 purified enzyme under strictly anaerobic conditions Eubacterium barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.291 2-formylglutarate + NADH + H+ the enzyme forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri Eubacterium barkeri 2-hydroxymethylglutarate + NAD+
-
 ?
1.1.1.291 2-hydroxymethylglutarate + NAD+
-
 Eubacterium barkeri 2-formylglutarate + NADH + H+
-
 r
1.3.7.1 6-hydroxynicotinate + reduced ferredoxin
-
 Eubacterium barkeri 1,4,5,6-tetrahydro-6-oxonicotinate + oxidized ferredoxin
-
 r
3.5.2.18 6-oxo-1,4,5,6-tetrahydronicotinate + H2O
-
 Eubacterium barkeri 2-formylglutarate + NH3
-
 r
3.5.2.18 6-oxo-1,4,5,6-tetrahydronicotinate + H2O the enzyme forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri Eubacterium barkeri 2-formylglutarate + NH3
-
 r
4.1.3.32 (2R,3S)-dimethylmalate
-
 Eubacterium barkeri propanoate + pyruvate
-
 ?
5.3.3.6 Methylitaconate
-
 Eubacterium barkeri Dimethylmaleate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.291 tetramer 4 * 32000, SDS-PAGE Eubacterium barkeri
1.3.7.1 homotetramer SDS-PAGE Eubacterium barkeri
3.5.2.18 tetramer 4 * 40000, SDS-PAGE Eubacterium barkeri
3.5.2.18 tetramer 4 * 39793, MALDI-TOF MS Eubacterium barkeri
4.1.3.32 homotetramer 4 * 31400, SDS-PAGE Eubacterium barkeri

Synonyms

EC Number Synonyms Comment Organism
1.1.1.291 HgD
-
 Eubacterium barkeri
4.1.3.32 (2R,3S)-dimethylmalate lyase
-
 Eubacterium barkeri
5.3.3.6 (R)-3-methylitaconate isomerase
-
 Eubacterium barkeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.291 NAD+ no activity with NADP+ Eubacterium barkeri
1.1.1.291 NADH
-
 Eubacterium barkeri