02040nas a2200241   4500008004100000022001400041245015900055210006900214260010300283300001400386490000700400520107700407653003401484653001301518653001701531653002101548653002301569653002401592653001301616100002401629700001401653856013101667       2007                        eng d  a0300-908400aBiochemical characterization of a novel beta-1-3, 1-4 glucan 4-glucanohydrolase from thermomonospora sp having a single active site for lichenan and xylan0 aBiochemical characterization of a novel beta13 14 glucan 4glucan  a23 RUE LINOIS, 75724 PARIS, FRANCEbELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIERcDEC  a1489-14970 v893 a<p>A bifunctional high molecular weight (Mr, 64,500 Da) beta-1-3, 1-4 glucan 4-glucanohydrolase was purified to homogeneity from Thermomonospora sp., exhibiting activity towards lichenan and xylan. A kinetic method was used to analyze the active site that hydrolyzes lichenan and xylan. The experimental data was in agreement with the theoretical values calculated for a single active site. Probing the conformation and microenvironment at active site of the enzyme by fluorescent chemo-affinity label, OPTA resulted in the formation of an isoindole derivative with complete inactivation of the enzyme to hydrolyse both lichenan and xylan confirmed the results of kinetic method. OPTA forms an isoindole derivative by cross-linking the proximal thiol and amino groups. The modification of cysteine and lysine residues by DTNB and TNBS respectively abolished the ability of the enzyme to form an isoindole derivative with OPTA, indicating the participation of cysteine and lysine in the formation of isoindole complex. (C) 2007 Elsevier Masson SAS. All rights reserved.</p>10a1-4 glucan 4-glucanohydrolase10abeta-1-310abifunctional10aO-phthaialdehyde10asingle active site10aThermomonospora sp.10aXylanase1 aAnish, Ramakrishnan1 aRao, Mala  uhttps://library.ncl.res.in/content/biochemical-characterization-novel-beta-1-3-1-4-glucan-4-glucanohydrolase-thermomonospora-0