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Purification and properties of glutamine synthetase from Hydrogenobacter thermophilus TK-6

Paper ID Volume ID Publish Year Pages File Format Full-Text
22023 43249 2006 5 PDF Available
Title
Purification and properties of glutamine synthetase from Hydrogenobacter thermophilus TK-6
Abstract

Hydrogenobacter thermophilus TK-6, a thermophilic and obligately chemoautotrophic bacterium, assimilates ammonium using glutamine synthetase (GS). GS was purified using three chromatography steps. The purified GS was found to belong to GS type I on the basis of its subunit composition and molecular weight. The Mg2+-dependent activity of this GS significantly increased after incubation with phosphodiesterase, indicating that GS is subject to adenylyl/deadenylyl regulation, a posttranslational modification system reported mainly among enterobacteria. The degree of this posttranslational modification changed depending on growth phase, confirming that adenylyl/deadenylyl regulation functions in vivo. Interestingly, the Km for glutamate of H. thermophilus GS was significantly higher than those of other organisms, suggesting that GS activity is affected by intracellular glutamate concentration.

Keywords
CFE; cell-free extract; GOGAT; glutamate synthase (glutamine:2-oxoglutarate amidotransferase); GS; glutamine synthetase; GSI; GS type I; RTCA cycle; reductive tricarboxylic acid cycleglutamine synthetase; Hydrogenobacter thermophilus; nitrogen assimilatio
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Purification and properties of glutamine synthetase from Hydrogenobacter thermophilus TK-6
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 102, Issue 4, October 2006, Pages 311–315
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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