Crystallization and preliminary X-ray diffraction analysis of<scp>L</scp>-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon<i>Thermococcus kodakaraensis</i>

Bowyer, A.; Mikolajek, Halina; Wright, James A.; Coker, Alun R.; Erskine, P.T.; Cooper, J.B.; Bashir, Qamar; Rashid, Naeem; Jamil, Farrukh; Akhtar, Muhammad

doi:10.1107/s1744309108025384

Cited by 3 publications

(2 citation statements)

References 15 publications

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“…TkTDH possesses 350 amino acid residues and has a molecular mass of 38,016 Da per monomer, as determined by electrospray mass spectrometry (Bowyer et al, 2008). As well as displaying high sequence similarity with other TDHs from hyperthermophiles (e.g.…”

Section: Primary Structure Similaritymentioning

confidence: 99%

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Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Bowyer

Mikolajek

Stuart

et al. 2009

Journal of Structural Biology

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Section: Primary Structure Similaritymentioning

confidence: 99%

“…The expression and purification of TkTDH was carried out according to the methods previously described in Bowyer et al (2008) and Bashir et al (2009). Recombinant pET-tdh plasmid was transformed and expressed in E. coli BL21 (DE3).…”

Section: Expression and Purificationmentioning

confidence: 99%

Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Bowyer

Mikolajek

Stuart

et al. 2009

Journal of Structural Biology

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Highly Thermostable L-Threonine Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis

Bashir

Rashid

Jamil

et al. 2009

Journal of Biochemistry

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l-Threonine dehydrogenase, a key enzyme in the l-threonine metabolism, catalyses the NAD(+)-dependent conversion of l-threonine to 2-amino-3-ketobutyrate, that non-enzymically decarboxylates to aminoacetone. A search of the genome sequence of hyperthermophilic archaeon, Thermococcus kodakaraensis revealed the presence of a closely related orthologue (TK0916) of archaeal and bacterial l-threonine dehydrogenase genes. Expression in Escherichia coli, purification and characterization of the TK0916 gene product revealed that this gene actually coded for a protein with high levels of l-threonine dehydrogenase activity (7.26 U mg(-1)). The enzyme exhibited highest activity at pH 12 and 90 degrees C. The K(m) values for l-threonine and NAD(+) at 50 degrees C were 1.6 mM and 0.028 mM, respectively. The enzyme activity was dependent on divalent cations. The half-life of the enzyme was more than 2 h at 85 degrees C and 24 min in boiling water. This is the most thermostable threonine dehydrogenase exhibiting optimal activity at the highest pH (12) reported to date. This is the first report on the characterization of a TDH from genus Thermococcus.

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Application of Phenotype Microarray for Profiling Carbon Sources Utilization between Biofilm and Non-Biofilm of Pseudomonas aeruginosa from Clinical Isolates

Ismail

Subbiah

Taib

2020

CPB

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: Pseudomonas aeruginosa a gram-negative bacterium with high versatility that can undergo aerobic and anaerobic respiration. Capabilities in deploying different carbon sources, energy metabolism, and regulatory system, ensure the survival of this microorganism in the diverse environmental conditions. Determination of differences in carbon sources utilization among biofilm and non-biofilm of P. aeruginosa provides a platform in understanding the metabolic activities of the microorganism. Three archived clinical isolates of strong, moderate, and non-biofilm producers were identified. ATCC 27853 P. aeruginosa was used as a negative control or non-biofilm producing microorganism. Biofilm formation of ATCC 27853 P. aeruginosa was confirmed by crystal violet assay (CVA) and Congo red agar (CRA). Metabolic profiles of the biofilm and non-biofilms isolates were determined by phenotype microarrays (Biolog Omnilog). In this study, the biofilm isolates utilized uridine, threonine, and serine while non-biofilm isolates utilized adenosine, inosine, monomethyl, sorbic acid, and succinamic acid. Sugar utilization was seen between the isolates adhering that biofilm P. aeruginosa preferred glucoside, galactoside, glucuronide, glucosaminide, mannoside, and galactosaminide, but it was not utilized by the non-biofilm. The outcome of this result can be used for future studies to improve detection or inhibition of the growth of clinical P. aeruginosa biofilm and non-biofilm, respectively.

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Crystallization and preliminary X-ray diffraction analysis ofL-threonine dehydrogenase (TDH) from the hyperthermophilic archaeonThermococcus kodakaraensis

Cited by 3 publications

References 15 publications

Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis

Highly Thermostable L-Threonine Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis

Application of Phenotype Microarray for Profiling Carbon Sources Utilization between Biofilm and Non-Biofilm of Pseudomonas aeruginosa from Clinical Isolates

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