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
Electron. j. biotechnol
;
12(3): 5-6, July 2009. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-551883
ABSTRACT
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.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Serratia marcescens
/
Gluconatos
Idioma:
Inglés
Revista:
Electron. j. biotechnol
Asunto de la revista:
Biotecnologia
Año:
2009
Tipo del documento:
Artículo
País de afiliación:
Corea del Sur
Institución/País de afiliación:
Dong-A University/KR
/
Dong-Ju College/KR
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