| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diacetyl | slight substrate inhibition, physiologically irrelevant | Shouchella clausii |
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics, Arrhenius plots permit the calculation of activation energies of 27 kJ/mol, 41 kJ/mol and 60 kJ/mol for the BDH catalyzed acetoin reductase, diacetyl reductase and butane-2,3-diol dehydrogenase activities, respectively | Shouchella clausii |
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required | Shouchella clausii |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diacetyl + NADH + H+ | Shouchella clausii | - |
(R)-acetoin + NAD+ | - |
ir | |
| diacetyl + NADH + H+ | Shouchella clausii DSM 8716 | - |
(R)-acetoin + NAD+ | - |
ir |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Shouchella clausii | A0A223LRZ7 | Bacillus clausii | - |
| Shouchella clausii DSM 8716 | A0A223LRZ7 | Bacillus clausii | - |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diacetyl + NADH + H+ | - |
Shouchella clausii | (R)-acetoin + NAD+ | - |
ir | |
| diacetyl + NADH + H+ | stereoselective reduction | Shouchella clausii | (R)-acetoin + NAD+ | - |
ir | |
| diacetyl + NADH + H+ | - |
Shouchella clausii DSM 8716 | (R)-acetoin + NAD+ | - |
ir | |
| diacetyl + NADH + H+ | stereoselective reduction | Shouchella clausii DSM 8716 | (R)-acetoin + NAD+ | - |
ir | |
| additional information | the two step reduction of diacetyl (butane-2,3-dione) with (R,R)-BDH solely yields (R,R)-butane-2,3-diol via (R)-acetoin, cf. EC 1.1.1.4. The enzyme catalyzes the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Starting with diacetyl as a substrate, exclusively (R,R)-butane-2,3-diol is formed. Bacillus clausii BDH catalyzes a highly selective oxidation of secondary alcohol groups in (R)-configuration of butane-2,3-diols and also reduces the carbonyl function in acetoin and diacetyl in a stereoselective manner to yield the (R)-configuration of the resulting chiral center, it selectively acts on vicinal diketones, alpha-hydroxy ketones and vicinal diols | Shouchella clausii | ? | - |
? | |
| additional information | the two step reduction of diacetyl (butane-2,3-dione) with (R,R)-BDH solely yields (R,R)-butane-2,3-diol via (R)-acetoin, cf. EC 1.1.1.4. The enzyme catalyzes the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Starting with diacetyl as a substrate, exclusively (R,R)-butane-2,3-diol is formed. Bacillus clausii BDH catalyzes a highly selective oxidation of secondary alcohol groups in (R)-configuration of butane-2,3-diols and also reduces the carbonyl function in acetoin and diacetyl in a stereoselective manner to yield the (R)-configuration of the resulting chiral center, it selectively acts on vicinal diketones, alpha-hydroxy ketones and vicinal diols | Shouchella clausii DSM 8716 | ? | - |
? |
| Synonyms | Comment | Organism |
|---|---|---|
| (R,R)-BDH | - |
Shouchella clausii |
| (R,R)-butane-2,3-diol dehydrogenase | - |
Shouchella clausii |
| (R,R)-butanediol dehydrogenase/diacetyl reductase | - |
Shouchella clausii |
| BdhA | - |
Shouchella clausii |
| additional information | see also EC 1.1.1.4 | Shouchella clausii |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
acetoin reductase, diacetyl reductase and butane-2,3-diol dehydrogenase activities show temperature optima at 50°C | Shouchella clausii |
| 50 | - |
diacetyl reductase activity optimum | Shouchella clausii |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
the pH-dependence of diacetyl reduction behaves quite differently from the acetoin reductase activity (optimum pH 7.0). The pH optimum is shifted down to pH 6.0, and the pH-dependence of activity is narrower as compared to the acetoin reductase activity | Shouchella clausii |
| 6 | - |
diacetyl reductase activity optimum | Shouchella clausii |
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Shouchella clausii |
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 330 | - |
diacetyl | pH 6.0, 50°C | Shouchella clausii |