chimeric construct C10 has a Ca2+ ion bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A
chimeric construct C10 has a Ca2+ ion bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 3.3fold activation of activity with carboxymethyl cellulose, 1.4fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 1.6fold activation of activity with carboxymethyl cellulose, 16.4% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 2.9fold activation of activity with carboxymethyl cellulose, 6.7% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 1.1fold activation of activity with carboxymethyl cellulose, 9.1% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 13% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 2.3fold activation of activity with carboxymethyl cellulose, 6.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
the removal of metals results into complete loss of enzymatic activity and is completely recovered in the presence of 1 mM Mn2+. 12fold activation at 1.5 mM Mn2+
5 mM, 6.6fold activation of activity with carboxymethyl cellulose, 1.6fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 6% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
the endoglucanase revealed a halotolerant profile since its activity increased proportionally to an increase in NaCl concentration. The maximum activity is reached at 2 M NaCl with a 75% increase in activity
the purified Bc22Cel shows a considerable halophilic property, being able to maintain more than 70% of residual activity when pre-incubated with 1.5 M NaCl for 1 h
5 mM, 1.7fold activation of activity with carboxymethyl cellulose, no effect on xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
the enzyme contains an unusual metal-ion site, which is originally modelled as a Ca2+ site (PDB ID 2xqo) but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. This metal-ion site can accommodate a range of transition metals, i.e. Fe2+, Cu2+, Mn2+ and Ni2+, but not Ca2+, whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue, a feature that is rarely observed but that is believed to be involved in an off-switch to transition-metal binding. Atomic resolution complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which is presumably present as a contaminant in the cellohexaose used for crystallization
the enzyme contains an unusual metal-ion site, which is originally modelled as a Ca2+ site (PDB ID 2xqo) but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. This metal-ion site can accommodate a range of transition metals, i.e. Fe2+, Cu2+, Mn2+ and Ni2+, but not Ca2+, whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue, a feature that is rarely observed but that is believed to be involved in an off-switch to transition-metal binding. Atomic resolution complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which is presumably present as a contaminant in the cellohexaose used for crystallization