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| Lee,Yong-Seok; Park,In-Hye; Yoo,Ju-Soon; Kim,Hae-Sun; Chung,Soo-Yeol; Chandra,Muni Ramanna GariSubhosh; Choi,Yong-Lark. |
| 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. |
| Tipo: Journal article |
Palavras-chave: 2-keto-3-deoxygluconate kinase; Carbohydrate kinase; Purification; Serratia marcescens KCTC 2172. |
| Ano: 2009 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582009000300005 |
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