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Literature summary extracted from

  • Bramski, J.; Dick, M.; Pietruszka, J.; Classen, T.
    Probing the acetaldehyde-sensitivity of 2-deoxy-ribose-5-phosphate aldolase (DERA) leads to resistant variants (2017), J. Biotechnol., 258, 56-58 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.4 expression in Escherichia coli BL21(DE3) Rhodococcus erythropolis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.4 C47A the mutant enzyme is highly sensitive to crotonaldehyde and acetaldehyde Rhodococcus erythropolis
4.1.2.4 C47G the mutant enzyme is highly sensitive to crotonaldehyde and acetaldehyde Rhodococcus erythropolis
4.1.2.4 C47L the mutant enzyme shows no loss in stereoselectivity, the mutant is fully resistant to inhibition by crotonaldehyde Rhodococcus erythropolis
4.1.2.4 C47M the mutant is both, the most acetaldehyde resistant variant and well performing on stereoselectivity, it is less resistant to crotonaldehyde than mutant C47M Rhodococcus erythropolis
4.1.2.4 C47S although serine is similar to cysteine, this variant is ten times more stable against acetaldehyde than the wildtype Rhodococcus erythropolis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.4 acetaldehyde
-
 Rhodococcus erythropolis
4.1.2.4 crotonaldehyde the enzyme produces crotonaldehyde as side reaction from acetaldehyde which is then an irreversible inhibitor forming a covalent Michael-adduct within the active site in particular with cysteine 47 Rhodococcus erythropolis

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.4 Rhodococcus erythropolis C0ZUQ6
-
-
4.1.2.4 Rhodococcus erythropolis NBRC 100887 C0ZUQ6
-
-

Synonyms

EC Number Synonyms Comment Organism
4.1.2.4 2-deoxy-D-ribose-5-phosphate aldolase
-
 Rhodococcus erythropolis
4.1.2.4 DeoC
-
 Rhodococcus erythropolis
4.1.2.4 DERA
-
 Rhodococcus erythropolis