Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Klebsiella pneumoniae |
Crystallization (Comment) | Organism |
---|---|
in complex with substrate meso-2,3-butanediol and inhibitor 2-mercaptoethanol, to 1.7 A resolution. The overall structure is similar to that of other short chain dehydrogenase/reductase enzymes, the NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. 2-Mercaptoethanol forms hydrogens bonds with residues Gln 140 and Gly 183 close to the active site, which are important but not sufficient for distiguishing stereoisomerism of a chiral substrate | Klebsiella pneumoniae |
Protein Variants | Comment | Organism |
---|---|---|
Q140I | mutation mimicking the corresponding residue in (S,S)-butanediol dehydrogenase. No activity with substrates meso-butanediol or (S,S)-butanediol | Klebsiella pneumoniae |
Q140I/N146F | mutation mimicking the corresponding residues in (S,S)-butanediol dehydrogenase. Poor activity with substrates meso-butanediol or (S,S)-butanediol | Klebsiella pneumoniae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | competitive | Klebsiella pneumoniae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(2R,3S)-butane-2,3-diol + NAD+ = acetoin + NADH + H+ | catalytic triad is formed by residues Ser139, Tyr 152, and Lys156 | Klebsiella pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
meso-2,3-butanediol + NAD+ | - |
Klebsiella pneumoniae | acetoin + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
meso-2,3-butanediol dehydrogenase | - |
Klebsiella pneumoniae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.52 | - |
2-mercaptoethanol | pH 8.0, temperature not specified in the publication | Klebsiella pneumoniae |