Gene expression and characterization of 2-keto-3-deoxy-gluconate kinase, a key enzyme in the modified Entner-Doudoroff pathway of Serratia marcescens KCTC 2172

We cloned 2-keto-3-deoxy-gluconate kinase (KDGK), which catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phophogluconate (KDPG) from Serratia marcescens KCTC 2172. The nucleotide sequence revealed a single open reading frame containing 1,208 bp and encoding for 309...

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Published inElectronic Journal of Biotechnology Vol. 12; no. 3; pp. 5 - 6
Main Authors Lee, Yong-Seok, Park, In-Hye, Yoo, Ju-Soon, Kim, Hae-Sun, Chung, Soo-Yeol, Chandra, Muni Ramanna GariSubhosh, Choi, Yong-Lark
Format Journal Article
LanguagePortuguese
Published Pontificia Universidad Católica de Valparaíso 01.07.2009
Subjects
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
carbohydrate kinase
purification
2-keto-3-deoxygluconate kinase
Serratia marcescens KCTC 2172
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Summary:We cloned 2-keto-3-deoxy-gluconate kinase (KDGK), which catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phophogluconate (KDPG) from Serratia marcescens KCTC 2172. The nucleotide sequence revealed a single open reading frame containing 1,208 bp and encoding for 309 amino acids, with a molecular weight of 33,993 Da. The enzyme was purified via GST affinity chromatography. The putative KdgT binding site was detected upstream of the initial codon. The KDG kinase utilized 2-ketogluconate (KG) and KDG as substrates. The optimal temperature and pH for KDGK activity were 50ºC and 8.0, respectively.
ISSN:0717-3458
0717-3458
DOI:10.4067/S0717-34582009000300005