Cloning of the cel 9A gene and characterization of its gene product from marine bacterium Pseudomonas sp. SK38

2001 ◽  
Vol 57 (1-2) ◽  
pp. 138-145 ◽  
Author(s):  
S. Ryu ◽  
S. Cho ◽  
S. Park ◽  
W. Lim ◽  
M. Kim ◽  
...  
Author(s):  
Keiko Kita ◽  
Shun-ichiro Mashiba ◽  
Masatoshi Nagita ◽  
Kaori Ishimaru ◽  
Kenji Okamoto ◽  
...  

Microbiology ◽  
2011 ◽  
Vol 157 (11) ◽  
pp. 3243-3251 ◽  
Author(s):  
Gerd M. Seibold ◽  
Katrin J. Breitinger ◽  
Raoul Kempkes ◽  
Leonard Both ◽  
Matthias Krämer ◽  
...  

Corynebacterium glutamicum transiently accumulates glycogen as carbon capacitor during the early exponential growth phase in media containing carbohydrates. In some bacteria glycogen is synthesized by the consecutive action of ADP-glucose pyrophosphorylase (GlgC), glycogen synthase (GlgA) and glycogen branching enzyme (GlgB). GlgC and GlgA of C. glutamicum have been shown to be necessary for glycogen accumulation in this organism. However, although cg1381 has been annotated as the putative C. glutamicum glgB gene, cg1381 and its gene product have not been characterized and their role in transient glycogen accumulation has not yet been investigated. We show here that the cg1381 gene product of C. glutamicum catalyses the formation of α-1,6-glycosidic bonds in polysaccharides and thus represents a glycogen branching enzyme. RT-PCR experiments revealed glgB to be co-transcribed with glgE, probably encoding a maltosyltransferase. Promoter activity assays with the glgE promoter region revealed carbon-source-dependent expression of the glgEB operon. Characterization of the growth and glycogen content of glgB-deficient and glgB-overexpressing strains showed that the glycogen branching enzyme GlgB is essential for glycogen formation in C. glutamicum. Taken together these results suggest that an interplay of the enzymes GlgC, GlgA and GlgB is not essential for growth, but is required for synthesis of the transient carbon capacitor glycogen in C. glutamicum.


2006 ◽  
Vol 72 (9) ◽  
pp. 6399-6401 ◽  
Author(s):  
Jinhua Dong ◽  
Shinnosuke Hashikawa ◽  
Takafumi Konishi ◽  
Yutaka Tamaru ◽  
Toshiyoshi Araki

ABSTRACT The β-agarase C gene (agaC) of a marine bacterium, Vibrio sp. strain PO-303, consisted of 1,437 bp encoding 478 amino acid residues. β-Agarase C was identified as the first β-agarase that cannot hydrolyze neoagarooctaose and smaller neoagarooligosaccharides and was assigned to a novel glycoside hydrolase family.


1991 ◽  
Vol 173 (4) ◽  
pp. 1452-1459 ◽  
Author(s):  
G S Gassmann ◽  
E Jacobs ◽  
R Deutzmann ◽  
U B Göbel

1999 ◽  
Vol 266 (3) ◽  
pp. 811-819 ◽  
Author(s):  
Satoru Watanabe ◽  
Tomonari Muramatsu ◽  
Hiroko Ao ◽  
Yoshie Hirayama ◽  
Kenji Takahashi ◽  
...  

1991 ◽  
Vol 638 (1 The Fibroblas) ◽  
pp. 400-402 ◽  
Author(s):  
KATHLEEN KEEGAN ◽  
DANIELE. JOHNSON ◽  
LEWIS T. WILLIAMS ◽  
MICHAEL J. HAYMAN
Keyword(s):  

1994 ◽  
Vol 19 (2) ◽  
pp. 117-129 ◽  
Author(s):  
B S Vijaya Gouri ◽  
V Rema ◽  
S Kamatkar ◽  
Ghansityam Swarup

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