Donor Substrate Specificity of 4- -Glucanotransferase of Porcine Liver Glycogen Debranching Enzyme and Complementary Action to Glycogen Phosphorylase on Debranching

2007 ◽  
Vol 143 (3) ◽  
pp. 435-440 ◽  
Author(s):  
Y. Watanabe ◽  
Y. Makino ◽  
K. Omichi
Keyword(s):  
Substrate Specificity ◽  
Glycogen Phosphorylase ◽  
Liver Glycogen ◽  
Porcine Liver ◽  
Debranching Enzyme ◽  
Donor Substrate ◽  
Complementary Action ◽  
Glycogen Debranching Enzyme

Structural rationale for the short branched substrate specificity of the glycogen debranching enzyme GlgX

2010 ◽  
Vol 78 (8) ◽  
pp. 1847-1855 ◽  
Author(s):  
Hyung-Nam Song ◽  
Tae-Yang Jung ◽  
Jong-Tae Park ◽  
Byung-Chul Park ◽  
Pyung Keun Myung ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Debranching Enzyme ◽  
Glycogen Debranching Enzyme

scholarly journals Enhanced Symbiotic Performance by Rhizobium tropici Glycogen Synthase Mutants

2001 ◽  
Vol 183 (3) ◽  
pp. 854-864 ◽  
Author(s):  
Silvia Marroquı́ ◽  
Angeles Zorreguieta ◽  
Carmen Santamarı́a ◽  
Francisco Temprano ◽  
Mario Soberón ◽  
...  
Keyword(s):  
Glycogen Phosphorylase ◽  
Symbiotic Nitrogen Fixation ◽  
Glycogen Synthase ◽  
Dry Weight ◽  
Gene Products ◽  
Branching Enzyme ◽  
Rhizobium Tropici ◽  
Debranching Enzyme ◽  
Glycogen Debranching Enzyme ◽  
Six Genes

ABSTRACT We isolated a Tn5-induced Rhizobium tropicimutant that has enhanced capacity to oxidizeN,N-dimethyl-p-phenylendiamine (DMPD) and therefore has enhanced respiration via cytochrome oxidase. The mutant had increased levels of the cytochromes c 1 and CycM and a small increase in the amount of cytochromeaa 3. In plant tests, the mutant increased the dry weight of Phaseolus vulgaris plants by 20 to 38% compared with the control strain, thus showing significantly enhanced symbiotic performance. The predicted product of the mutated gene is homologous to glycogen synthases from several bacteria, and the mutant lacked glycogen. The DNA sequence of the adjacent gene region revealed six genes predicted to encode products homologous to the following gene products from Escherichia coli: glycogen phosphorylase (glgP), glycogen branching enzyme (glgB), ADP glucose pyrophosphorylase (glgC), glycogen synthase (glgA), phosphoglucomutase (pgm), and glycogen debranching enzyme (glgX). All six genes are transcribed in the same direction, and analysis with lacZ gene fusions suggests that the first five genes are organized in one operon, although pgm appears to have an additional promoter;glgX is transcribed independently. Surprisingly, theglgA mutant had decreased levels of high-molecular-weight exopolysaccharide after growth on glucose, but levels were normal after growth on galactose. A deletion mutant was constructed in order to generate a nonpolar mutation in glgA. This mutant had a phenotype similar to that of the Tn5 mutant, indicating that the enhanced respiration and symbiotic nitrogen fixation and decreased exopolysaccharide were due to mutation of glgAand not to a polar effect on a downstream gene.

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