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Characterization of the Glycogen Branching Enzyme from Pectobacterium carotovorum subsp carotovorum LY34
- Authors
- Lee, Young Han; Kim, Sung Kyum; Kim, Yong Ho; Kim, Eun Ju; Cho, Kye Man; Yun, Myoung Geun; Cho, Ji Joong; Kim, Jong Min; Yun, Han Dae; Kim, Hoon
- Issue Date
- Feb-2010
- Publisher
- KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
- Keywords
- GlgB; glycogen branching enzyme; glycogen debranching enzyme; Pectobacterium carotovorum subsp carotovorum LY34
- Citation
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.53, no.1, pp 78 - 88
- Pages
- 11
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
- Volume
- 53
- Number
- 1
- Start Page
- 78
- End Page
- 88
- ISSN
- 1738-2203
2234-344X
- Abstract
- A branching enzyme (EC 2.4.1.18) gene was isolated from Pectobacterium carotovorum subsp. carotovorum LY34. The branching enzyme gene, glgB, consists of an open reading frame (ORF) of 2,178 bp encoding a protein of 725 amino acids (calculated molecular weight of 83,891 Da). The ORF of the glgB gene starts with an ATG codon and ends with a TAA stop codon 3 bp upstream of glgX. The deduced amino acid sequence of GlgB has 40 to 95% similarity to known bacterial branching enzyme sequences. The enzyme is most similar to GlgB of Escherichia coli and contains the four regions conserved in the alpha-amylase family. The enzyme GlgB was purified and the molecular weight of the enzyme is estimated to be about 84 kDa. The glycogen branching enzyme is optimally active at pH 7 and 40 degrees C.
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