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Literature summary for 3.5.2.18 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
Search for more literature for 3.5.2.18

Metals/Ions

Metals/Ions Comment Organism Structure
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
additional information the enzyme contains the typical metal binding His-X-His pattern in the N-terminal part Eubacterium barkeri
Zn contains about 0.6 Zn per subunit Eubacterium barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39793
-
 4 * 39793, MALDI-TOF MS Eubacterium barkeri
40000
-
 4 * 40000, SDS-PAGE Eubacterium barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Eubacterium barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Eubacterium barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-oxo-1,4,5,6-tetrahydronicotinate + H2O
-
 Eubacterium barkeri 2-formylglutarate + NH3
-
 r
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

Subunits

Subunits Comment Organism
tetramer 4 * 40000, SDS-PAGE Eubacterium barkeri
tetramer 4 * 39793, MALDI-TOF MS Eubacterium barkeri