Cloning and characterization of Thermotoga maritima β-glucuronidase

The putative β-glucuronidase from Thermotoga maritima, comprising 563 amino acid residues conjugated with a Hisx6 tag, was cloned and expressed in Escherichia coli. The enzyme has a moderately broad specificity, hydrolysing a range of p-nitrophenyl glycoside substrates, but has greatest activity on...

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Veröffentlicht in:	Carbohydrate research 2006-01, Vol.341 (1), p.49-59
Hauptverfasser:	Salleh, Hamzah M., Müllegger, Johannes, Reid, Stephen P., Chan, Wing Y., Hwang, Jiyoung, Warren, R. Antony J., Withers, Stephen G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active site Amino Acid Sequence Animals Binding Sites Circular Dichroism Cloning, Molecular - methods Enzyme Stability Escherichia coli - enzymology Glucuronidase Glucuronidase - antagonists & inhibitors Glucuronidase - biosynthesis Glucuronidase - genetics Hot Temperature Humans Kinetics Labeling Mechanism Molecular Sequence Data Mutation Sequence Alignment Spectrometry, Mass, Electrospray Ionization Substrate Specificity Thermostable glycosidase Thermotoga maritima - enzymology
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