Crystallization (Comment) | Organism |
---|---|
in complex with NAD+ and 2-mercaptoethanol, to 2.0 A resolution. The L-BDH subunit is composed of seven beta-strands, six alpha-helices and two short a helices, aFG1 and aFG2, which form a small lobe on top of the core domain. The conserved active site residues Asn112, Ser141, Tyr154 and Lys158 are located near the NAD+ molecule | Corynebacterium glutamicum |
Protein Variants | Comment | Organism |
---|---|---|
F148N | trace activity below 0.1 U/mg | Corynebacterium glutamicum |
I142Q | trace activity below 0.1 U/mg | Corynebacterium glutamicum |
I142Q/F148N | trace activity below 0.1 U/mg | Corynebacterium glutamicum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | competitive. In crystal structure, the mercaptoethanol molecule is located in the catalytic cleft formed by residues Ser141, Ileu142, Ala143, Phe148, Tyr154, Pro184, Gly185, Ileu186, Met191, Trp192 and Ile195. These residues may also be involved in substrate recognition and in stereospecific redox reactions | Corynebacterium glutamicum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | Q9ZNN8 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.1 | - |
substrate meso-2,3-butanediol, pH 8.0, 37°C | Corynebacterium glutamicum |
4.3 | - |
substrate (2S,3S)-2,3-butanediol, pH 8.0, 37°C | Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2S,3S)-2,3-butanediol + NAD+ | - |
Corynebacterium glutamicum | (3S)-acetoin + NADH + H+ | - |
? | |
meso-2,3-butanediol + NAD+ | poor substrate | Corynebacterium glutamicum | acetoin + NADH | - |
? |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
4.3 | - |
2-mercaptoethanol | pH 8.0, 37°C | Corynebacterium glutamicum |