| dc.creator | Lee,Yong-Seok | |
| dc.creator | Park,In-Hye | |
| dc.creator | Yoo,Ju-Soon | |
| dc.creator | Kim,Hae-Sun | |
| dc.creator | Chung,Soo-Yeol | |
| dc.creator | Chandra,Muni Ramanna GariSubhosh | |
| dc.creator | Choi,Yong-Lark | |
| dc.date | 2009-07-01 | |
| dc.date.accessioned | 2019-05-03T12:44:37Z | |
| dc.date.available | 2019-05-03T12:44:37Z | |
| dc.identifier | https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582009000300005 | |
| dc.identifier.uri | http://revistaschilenas.uchile.cl/handle/2250/85075 | |
| dc.description | 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. | |
| dc.format | text/html | |
| dc.language | en | |
| dc.publisher | Pontificia Universidad Católica de Valparaíso | |
| dc.relation | 10.4067/S0717-34582009000300005 | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.source | Electronic Journal of Biotechnology v.12 n.3 2009 | |
| dc.subject | 2-keto-3-deoxygluconate kinase | |
| dc.subject | carbohydrate kinase | |
| dc.subject | purification | |
| dc.subject | Serratia marcescens KCTC 2172 | |
| dc.title | 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 | |
