search
for
 About Bioline  All Journals  Testimonials  Membership  News  Donations


Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 12, No. 3, 2009
Bioline Code: ej09025
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 12, No. 3, 2009

 en Gene expression and characterization of 2-keto-3-deoxy-gluconate kinase, a key enzyme in the modified Entner-Doudoroff pathway of Serratia marcescens check for this species in other resources KCTC 2172
Lee, Y.-S.; Park, I.-H.; Yoo, J.-S.; Kim, H.-S.; Chung, S.-Y.; Chandra, M.S. & Choi, Y.-L.

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 check for this species in other resources 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.

Keywords
2-keto-3-deoxygluconate kinase, carbohydrate kinase, purification, Serratia marcescens KCTC 2172.

 
© Copyright 2009 - Pontificia Universidad Católica de Valparaíso -- Chile
Alternative site location: http://www.ejbiotechnology.info

Home Faq Resources Email Bioline
© Bioline International, 1989 - 2017, Site last up-dated on 16-Oct-2017.
Site created and maintained by the Reference Center on Environmental Information, CRIA, Brazil
System hosted by the Internet Data Center of Rede Nacional de Ensino e Pesquisa, RNP, Brazil