Application | Comment | Organism |
---|---|---|
synthesis | biosynthesis of 2-deoxysugars using whole-cell catalyst expressing 2-deoxy-D-ribose 5-phosphate aldolase. A whole-cell transformation strategy using resting cells of the BL21(pKDERA12) strain, containing the expressed plasmid pKDERA12 (S238D/F200I/DELTAY259), results in increase in 2-deoxy-D-ribose yield from 0.41 mol/mol D-glyceraldehyde to 0.81 mol/mol D-glyceraldehyde and higher substrate tolerance from 0.5 to 3 M compared to in vitro assays. With further optimization of the transformation process, the BL21(pKDERA12) strain produces 2.14 M (287.06 g/l) 2-deoxy-D-ribose, with a yield of 0.71 mol/mol D-glyceraldehyde and average productivity of 0.13 mol/l*h (17.94 g/l*h). The results demonstrate the potential for large-scale production of 2-deoxy-D-ribose using the BL21(pKDERA12) strain. Furthermore, the BL21(pKDERA12) strain also exhibits the ability to efficiently produce 2-deoxy-D-altrose from D-erythrose, as well as 2-deoxy-L-xylose and 2-deoxy-L-ribose from L-glyceraldehyde | Klebsiella pneumoniae |
Protein Variants | Comment | Organism |
---|---|---|
F165I | mutant enzyme shows 87.5 % of the activity of wild-type enzyme, preferable substrate tolerance compared with wild-type enzyme KDERA when the reactions are performed with 200 mM D-glyceraldehyde and acetaldehyde | Klebsiella pneumoniae |
F200I | 2.4fold improvement in enzyme activities compared to wild-type enzyme, preferable substrate tolerance compared with wild-type enzyme KDERA when the reactions are performed with 200 mM D-glyceraldehyde and acetaldehyde | Klebsiella pneumoniae |
F200I/DELTAY259 | substrate tolerance of the mutant enzyme is 37.3 % higher than that of wild-type enzyme | Klebsiella pneumoniae |
G171S | inactive mutant enzyme | Klebsiella pneumoniae |
L20D | inactive mutant enzyme | Klebsiella pneumoniae |
M185V | 1.8fold improvement in enzyme activities compared to wild-type enzyme, preferable substrate tolerance compared with wild-type enzyme KDERA when the reactions are performed with 200 mM D-glyceraldehyde and acetaldehyde | Klebsiella pneumoniae |
S238D/F200I/DELTAY259 | 3.15fold improvement in enzyme activity and a 1.54fold increase in substrate tolerance towards D-glyceraldehyde compared with the wild type | Klebsiella pneumoniae |
T168L | mutant enzyme is virtually inactive | Klebsiella pneumoniae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetaldehyde | the activity of wild-type enzyme sharply dropps by 43 % under 200 mM D-glyceraldehyde and acetaldehyde, which limits its large-scale synthetic applications | Klebsiella pneumoniae | |
D-glyceraldehyde | the activity of wild-type enzyme sharply dropps by 43 % under 200 mM D-glyceraldehyde and acetaldehyde, which limits its large-scale synthetic applications | Klebsiella pneumoniae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella pneumoniae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Klebsiella pneumoniae |
Synonyms | Comment | Organism |
---|---|---|
2-deoxy-D-ribose 5-phosphate aldolase | - |
Klebsiella pneumoniae |
DERA | - |
Klebsiella pneumoniae |