2021
DOI: 10.1007/s00253-021-11462-0
|View full text |Cite
|
Sign up to set email alerts
|

Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact

Abstract: Deoxyribose-5-phosphate aldolases (DERAs, EC 4.1.2.4) are acetaldehyde-dependent, Class I aldolases catalyzing in nature a reversible aldol reaction between an acetaldehyde donor (C2 compound) and glyceraldehyde-3-phosphate acceptor (C3 compound, C3P) to generate deoxyribose-5-phosphate (C5 compound, DR5P). DERA enzymes have been found to accept also other types of aldehydes as their donor, and in particular as acceptor molecules. Consequently, DERA enzymes can be applied in C–C bond formation reactions to pro… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
10
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
5
1

Relationship

0
6

Authors

Journals

citations
Cited by 10 publications
(10 citation statements)
references
References 72 publications
0
10
0
Order By: Relevance
“…Natural aldolases are regarded as highly specific for their nucleophilic aldol donor and are restricted by the range of reactions catalyzed. Even though the substrate scope, activity, and stability , of the archetypical class I aldolase DERA have been successfully altered to enlarge its usefulness for diverse aldol reactions, examples of other mechanistically related carboligation reactions catalyzed by DERA are unknown. In the current study, we demonstrate that the active site of DERA from E.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Natural aldolases are regarded as highly specific for their nucleophilic aldol donor and are restricted by the range of reactions catalyzed. Even though the substrate scope, activity, and stability , of the archetypical class I aldolase DERA have been successfully altered to enlarge its usefulness for diverse aldol reactions, examples of other mechanistically related carboligation reactions catalyzed by DERA are unknown. In the current study, we demonstrate that the active site of DERA from E.…”
Section: Discussionmentioning
confidence: 99%
“…Natural aldolases are regarded as highly specific for their nucleophilic aldol donor 7 and are restricted by the range of reactions catalyzed. Even though the substrate scope, activity, and stability [8][9][10][11][12]39 of the archetypical class I aldolase DERA have been successfully altered to enlarge its usefulness for diverse aldol reactions, examples of other mechanistically related carboligation reactions catalyzed by DERA are unknown. In the current study, we demonstrate that the active site of DERA from E. coli can give rise to synthetically useful catalytic promiscuity, supporting asymmetric Michael additions of nitromethane to various α,β-unsaturated aldehydes to give γ-nitroaldehydes, important chiral synthons for pharmaceutically active γ-aminobutyric acids.…”
Section: ■ Conclusionmentioning
confidence: 99%
“…Therefore, in the last decades considerable attention has been paid to the search for new aldolases from a large diversity of microorganisms with enhanced acetaldehyde resistance. [28,29,22] In a previous work we selected DERA from P. atrosepticum (PaDERA) as an efficient wild-type bacterial whole cell biocatalyst for its ability to synthesize DR5P at up to 200 mM of acetaldehyde. [26] In addition, DR5P was further employed in an one-pot multistep enzymatic synthesis to prepare thymidine.…”
Section: Dr5p Productionmentioning
confidence: 99%
“…Following this strategy, different recombinant DERAs have been reported with the aim of increasing their tolerance to high aldehyde concentrations. [22] DERA has been shown to have a low preference for nonphosphorylated substrates. [23] In order to overcome this, De Santis et al, prepared a mutant of E. coli DERA (S238D) with improved activity towards 2-deoxy-D-ribose.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation