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Literature summary for 4.1.2.4 extracted from

  • Li, J.; Yang, J.; Men, Y.; Zeng, Y.; Zhu, Y.; Dong, C.; Sun, Y.; Ma, Y.
    Biosynthesis of 2-deoxysugars using whole-cell catalyst expressing 2-deoxy-D-ribose 5-phosphate aldolase (2015), Appl. Microbiol. Biotechnol., 99, 7963-7972 .
    View publication on PubMed

Application

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

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

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

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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-
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Purification (Commentary)

Purification (Comment) Organism
-
Klebsiella pneumoniae

Synonyms

Synonyms Comment Organism
2-deoxy-D-ribose 5-phosphate aldolase
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Klebsiella pneumoniae
DERA
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Klebsiella pneumoniae