Application | Comment | Organism |
---|---|---|
synthesis | introduction of a 2-hydroxyisobutyric acid synthesis route in Escherichia coli by concomitantly expressing the RCM genes and phaA and phaB, encoding beta-ketothiolase and NADP-dependent (R)-3-hydroxybutyryl-CoA dehydrogenase. A concentration of 3-hydroxybutyric acid of up to 17.7 mM can be obtained within 8 days of feeding the recombinant strain with gluconic acid as the main carbon source | Kyrpidia tusciae DSM 2912 |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Kyrpidia tusciae DSM 2912 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.087 | - |
(R)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
0.09 | - |
2-hydroxyisobutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
0.313 | - |
(S)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Kyrpidia tusciae DSM 2912 | D5WTR7 and D5WTR8 | D5WTR7 i.e. subunit RcmA, D5WTR8 i.e. subunit RcmB | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-3-hydroxybutanoyl-CoA | catalytic efficiency for the (R)-enantiomer is about 11 times higher than for the (S)-enantiomer | Kyrpidia tusciae DSM 2912 | 2-hydroxybutanoyl-CoA | - |
r | |
(S)-3-hydroxybutanoyl-CoA | catalytic efficiency for the (R)-enantiomer is about 11 times higher than for the (S)-enantiomer | Kyrpidia tusciae DSM 2912 | 2-hydroxybutanoyl-CoA | - |
r | |
2-hydroxyisobutanoyl-CoA | - |
Kyrpidia tusciae DSM 2912 | (S)-3-hydroxyisobutanoyl-CoA + (R)-3-hydroxyisobutanoyl-CoA | - |
r | |
additional information | (R)-3-hydroxybuytryl-CoA is converted 3.1 times faster than the (S)-enantiomer | Kyrpidia tusciae DSM 2912 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
multimer | x * subunit RcmA + x * subunit RcmB | Kyrpidia tusciae DSM 2912 |
Synonyms | Comment | Organism |
---|---|---|
Btus_0469 | gene name, subunit RcmA | Kyrpidia tusciae DSM 2912 |
Btus_0470 | gene name, subunit RcmB | Kyrpidia tusciae DSM 2912 |
RcmA | - |
Kyrpidia tusciae DSM 2912 |
RcmB | - |
Kyrpidia tusciae DSM 2912 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
- |
Kyrpidia tusciae DSM 2912 |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
25% of maximum activity | Kyrpidia tusciae DSM 2912 |
75 | - |
55% of maximum activity | Kyrpidia tusciae DSM 2912 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.6 | - |
(S)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
3.7 | - |
2-hydroxyisobutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
4.9 | - |
(R)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
- |
Kyrpidia tusciae DSM 2912 |
General Information | Comment | Organism |
---|---|---|
malfunction | mutase from strain DSM 2912 catalyzes isomerization of (R)-3-hydroxybutanoyl-CoA about 7000 times more efficiently than the mutase from Aquincola tertiaricarbonis L108. The most striking structural difference between the two mutases, likely determining stereospecificity, is a replacement of active-site residue Asp found in strain L108 at position 117 with Val in the enzyme from strain DSM 2912, resulting in a reversed polarity at this binding site | Kyrpidia tusciae DSM 2912 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5 | - |
(S)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
40 | - |
2-hydroxyisobutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 | |
56.7 | - |
(R)-3-hydroxybutanoyl-CoA | pH 7.8, 55°C | Kyrpidia tusciae DSM 2912 |