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

• Yong-Seok Lee ^[1] ; In-Hye Park ^[1] ; Ju-Soon Yoo ^[2] ; Hae-Sun Kim ^[1] ; Soo-Yeol Chung ^[2] ; Muni Ramanna GariSubhosh Chandra ^[1] ; Yong-Lark Choi ^[1]
  1. [1] Dong-A University

     Dong-A University

     Corea del Sur

     
  2. [2] Dong-Ju College Department of Food Science and Nutrition
• Localización: Electronic Journal of Biotechnology, ISSN-e 0717-3458, Vol. 12, Nº. 3, 2009, págs. 5-6
• Idioma: inglés
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• Resumen

  • 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.