EC Number   |
General Information |
Reference |
|---|
    2.3.1.247 | evolution |
gene cluster organization in putative lysine-fermenting bacteria, overview |
-, 680885 |
| 2.3.1.247 | evolution |
the enzyme is a representative of a large family of prokaryotic hypothetical proteins, annotated as the domain of unknown function DUF849, it shows the ubiquitous triose phosphate isomerase (TIM) barrel fold and a Zn2+ cation reminiscent of metal-dependent class II aldolases |
734167 |
| 2.3.1.247 | metabolism |
C-1 and C-2 of 3-oxo-5-aminohexanoate are converted mainly to acetoacetate and acetate, whereas C-3 to C-6 are converted mainly to 3-hydroxybutyrate or its coenzyme A thiolester. 3-Aminobutyryl-CoA is then deaminated to form crotonyl-CoA. The enzymes observed in extracts of Brevibacterium sp. can account for the conversion of 3,5-diaminohexanoate to acetyl-CoA, overview |
-, 6044 |
| 2.3.1.247 | metabolism |
the enzyme is involved in the anaerobic fermentation of lysine |
734167 |
| 2.3.1.247 | metabolism |
the enzyme is involved in the fermentation pathway of lysine |
-, 680885 |
| 2.3.1.247 | metabolism |
the enzyme is involved in the the 3-keto-5-aminohexanoate pathway of lysine degradation, tracer experiments on acetate and butyrate formation from lysine and acetate, overview |
-, 3378 |
| 2.3.1.247 | more |
enzyme structure determination and analysis, the active site is situated in each monomer at the C-terminal face of the central beta-barrel with a metal ion coordinated by His46, His48, and Glu230, overview |
734167 |
