Protein Expression and Purification 2009-12-01

Cloning, expression, and characterization of a new deoxyribose 5-phosphate aldolase from Yersinia sp. EA015.

Yong-Mo Kim, Young-Hyo Chang, Nack-Shick Choi, Yongook Kim, Jae Jun Song, Joong Su Kim, Yong-Mo Kim, Young-Hyo Chang, Nack-Shick Choi, YongOok Kim, Jae Jun Song, Joong Su Kim

Index: Protein Expr. Purif. 68(2) , 196-200, (2009)

Full Text: HTML

Abstract

A new deoC gene encoding deoxyribose 5-phosphate aldolase (DERA) was identified in Yersinia sp. EA015 isolated from soil. The DERA gene had an open reading frame (ORF) of 672 base pairs encoding 223 amino acids to yield a protein of molecular mass 24.8 kDa. The amino acid sequence was 94% identical to that of DERA from Yersinia intermedia ATCC 29909. DERA was over-expressed in Escherichia coli and purified using Ni-NTA affinity chromatography. The specific activity was 137 micromol/min/mg. The Michaelis constant (k(m) value) of DERA was 9.1 mM. DERA was optimally active at pH 6.0 and 50 degrees C. DERA was tolerant to a high concentration (300 mM) of acetaldehyde.


Related Compounds

Related Articles:

Toxoplasma gondii: Identification and characterization of bradyzoite-specific deoxyribose phosphate aldolase-like gene (TgDPA).

2009-01-01

[Exp. Parasitol. 121(1) , 55-63, (2009)]

The fed-batch production of a thermophilic 2-deoxyribose-5-phosphate aldolase (DERA) in Escherichia coli by exponential feeding strategy control.

2010-11-01

[Appl. Biochem. Biotechnol. 162(5) , 1423-34, (2010)]

Automated clustering of ensembles of alternative models in protein structure databases.

2004-06-01

[Protein Eng. Des. Sel. 17(6) , 537-43, (2004)]

Efficient production of a thermophilic 2-deoxyribose-5-phosphate aldolase in glucose-limited fed-batch cultivations of Escherichia coli by continuous lactose induction strategy.

2011-09-01

[Appl. Biochem. Biotechnol. 165(2) , 416-25, (2011)]

Selection of a new whole cell biocatalyst for the synthesis of 2-deoxyribose 5-phosphate.

2012-01-01

[Appl. Biochem. Biotechnol. 166(2) , 300-8, (2012)]

More Articles...