DERA

Deoxyribose-Phosphate Aldolase E.Coli Recombinant
Cat. No.
BT26624
Source
Escherichia Coli.
Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

DERA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 29.9kDa.
DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. It catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and acetaldehyde.
Description
DERA, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 279 amino acids (amino acids 1-259) and has a molecular mass of 29.9 kDa. It is fused to a 20 amino acid His-tag at the N-terminus and purified by proprietary chromatographic techniques.
Physical Appearance
Sterile filtered colorless solution.
Formulation
The DERA solution is supplied at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 2 mM DTT.
Stability
For short-term storage (2-4 weeks), store the solution at 4°C. For long-term storage, freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Greater than 95% purity as determined by SDS-PAGE.
Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH GDGKSASSY.

Product Science Overview

Structure and Function

DERA is a member of the Class I aldolases, which are acetaldehyde-dependent enzymes. It catalyzes a reversible aldol reaction between an acetaldehyde donor (a C2 compound) and a glyceraldehyde-3-phosphate acceptor (a C3 compound) to generate deoxyribose-5-phosphate (a C5 compound) . This reaction is essential for the formation of carbon-carbon (C–C) bonds, making DERA a versatile biocatalyst for synthetic applications .

Recombinant Production

The recombinant form of DERA produced in Escherichia coli (E. coli) is a single, non-glycosylated polypeptide chain containing 338 amino acids and has a molecular mass of approximately 37.3 kDa . This recombinant enzyme is often fused to a His-tag at the N-terminus to facilitate purification through chromatographic techniques .

Applications and Engineering

DERA enzymes have been extensively studied and engineered to improve their substrate specificity, enzyme efficiency, and stability. Protein engineering strategies, including structure-based design, directed evolution, and machine learning-guided approaches, have been employed to optimize these enzymes . These engineered enzymes have shown improved activity towards various aldehyde substrates, including acetaldehyde and formaldehyde .

The synthetic utility of DERA enzymes extends to the production of novel compounds through C–C bond formation reactions. These enzymes have been applied in the synthesis of commodity chemicals, flavors, and high-value pharmaceutical compounds . For instance, DERA is the only known aldolase that accepts two aldehyde substrates, making it an attractive catalyst for synthesizing chiral polyol motifs present in pharmaceuticals like atorvastatin and pravastatin .

Future Prospects

The future of DERA enzyme engineering looks promising, with computational methods expected to accelerate the development of more efficient and stable variants . The use of enzyme immobilization and whole-cell catalysis is also anticipated to enhance the overall performance of biocatalytic processes .

In summary, Deoxyribose-Phosphate Aldolase from E. coli is a versatile and valuable enzyme with significant applications in synthetic chemistry and biotechnology. Its recombinant production and engineering have paved the way for innovative solutions in various industrial processes.

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