scholarly journals The Role of Conserved Arginine Residue in Loop 4 of Glycoside Hydrolase Family 10 Xylanases

2005 ◽  
Vol 69 (5) ◽  
pp. 904-910 ◽  
Author(s):  
Mamoru NISHIMOTO ◽  
Motomitsu KITAOKA ◽  
Shinya FUSHINOBU ◽  
Kiyoshi HAYASHI
Keyword(s):  
Glycoside Hydrolase ◽  
Arginine Residue ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 10 ◽  
Hydrolase Family

scholarly journals Substrate Specificity in Glycoside Hydrolase Family 10

2000 ◽  
Vol 275 (30) ◽  
pp. 23020-23026 ◽  
Author(s):  
Valérie Ducros ◽  
Simon J. Charnock ◽  
Urszula Derewenda ◽  
Zygmunt S. Derewenda ◽  
Zbigniew Dauter ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 10 ◽  
Hydrolase Family

scholarly journals Comparative Quantitative Analysis of Gene Expression Profiles of Glycoside Hydrolase Family 10 Xylanases in the Sheep Rumen during a Feeding Cycle

2012 ◽  
Vol 79 (4) ◽  
pp. 1212-1220 ◽  
Author(s):  
Zhongyuan Li ◽  
Heng Zhao ◽  
Peilong Yang ◽  
Junqi Zhao ◽  
Huoqing Huang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Glycoside Hydrolase ◽  
Expression Profiles ◽  
Expression Patterns ◽  
Functional Genes ◽  
Glycoside Hydrolase Family ◽  
Transcriptional Level ◽  
Glycoside Hydrolase Family 10 ◽  
Feeding Cycle ◽  
Hydrolase Family

ABSTRACTXylanase is a crucial hydrolytic enzyme that degrades plant polysaccharides in the rumen. To date, there is no information on the genetic composition and expression characteristics of ruminal xylanase during feeding cycles of ruminants. Here, the major xylanase of the glycoside hydrolase family 10 (GH 10) from the rumen of small-tail Han sheep was investigated during a feeding cycle. We identified 44 distinct GH 10 xylanase gene fragments at both the genomic and transcriptional levels. Comparison of their relative abundance showed that results from the evaluation of functional genes at the transcriptional level are more reliable indicators for understanding fluctuations in xylanase levels. The expression patterns of six xylanase genes, detected at all time points of the feeding cycle, were investigated; we observed a complex trend of gene expression over 24 h, revealing the dynamic expression of xylanases in the rumen. Further correlation analysis indicated that the rumen is a dynamic ecosystem where the transcript profiles of xylanase genes are closely related to ruminal conditions, especially rumen pH and bacterial population. Given the huge diversity and changing composition of enzymes over the entire rumen, this research provides valuable information for understanding the role of functional genes in the digestion of plant material.

Global and grain-specific accumulation of glycoside hydrolase family 10 xylanases in transgenic maize (Zea mays)

2011 ◽  
Vol 9 (9) ◽  
pp. 1100-1108 ◽  
Author(s):  
Benjamin N. Gray ◽  
Oleg Bougri ◽  
Alvar R. Carlson ◽  
Judy Meissner ◽  
Shihao Pan ◽  
...  
Keyword(s):  
Zea Mays ◽  
Glycoside Hydrolase ◽  
Transgenic Maize ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 10 ◽  
Specific Accumulation ◽  
Hydrolase Family

scholarly journals The Membrane-Bound α-Glucuronidase from Pseudomonas cellulosa Hydrolyzes 4-O-Methyl-d-Glucuronoxylooligosaccharides but Not 4-O-Methyl-d-Glucuronoxylan

2002 ◽  
Vol 184 (17) ◽  
pp. 4925-4929 ◽  
Author(s):  
Tibor Nagy ◽  
Kaveh Emami ◽  
Carlos M. G. A. Fontes ◽  
Luis M. A. Ferreira ◽  
David R. Humphry ◽  
...  
Keyword(s):  
Microbial Degradation ◽  
Glycoside Hydrolase ◽  
Glucuronic Acid ◽  
Biological Process ◽  
Glycoside Hydrolase Family ◽  
Membrane Bound ◽  
Primary Structures ◽  
Hydrolase Family

ABSTRACT The microbial degradation of xylan is a key biological process. Hardwood 4-O-methyl-d-glucuronoxylans are extensively decorated with 4-O-methyl-d-glucuronic acid, which is cleaved from the polysaccharides by α-glucuronidases. In this report we describe the primary structures of the α-glucuronidase from Cellvibrio mixtus (C. mixtus GlcA67A) and the α-glucuronidase from Pseudomonas cellulosa (P. cellulosa GlcA67A) and characterize P. cellulosa GlcA67A. The primary structures of C. mixtus GlcA67A and P. cellulosa GlcA67A, which are 76% identical, exhibit similarities with α-glucuronidases in glycoside hydrolase family 67. The membrane-associated pseudomonad α-glucuronidase released 4-O-methyl-d-glucuronic acid from 4-O-methyl-d-glucuronoxylooligosaccharides but not from 4-O-methyl-d-glucuronoxylan. We propose that the role of the glucuronidase, in combination with cell-associated xylanases, is to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-d-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers.

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