@article { ISI:000227415700018,
	title = {Purification and properties of a low molecular weight 1,4-beta-D-glucan glucohydrolase having one active site for carboxymethyl cellulose and xylan from an alkalothermophilic Thermomonospora sp},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {329},
	number = {1},
	year = {2005},
	month = {APR},
	pages = {111-116},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	type = {Article},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>A low molecular weight 1,4-beta-D-glucan glucohydrolase from an extracellular culture filtrate of Thermomonospora sp. was purified to homogeneity. The molecular weight of the purified enzyme was 14.2 kDa by MALDI-TOF analysis and is in agreement with SDS-PAGE and gel filtration chromatography. The purified enzyme exhibited both endocarboxymethyl cellulase and endoxylanase activities. A kinetic method was employed to study the active site of the enzyme that hydrolyzes both carboxymethyl cellulose and xylan. The experimental data coincide well with the theoretical values calculated for the case of a single active site. Conformation and microenvironment at the active site was probed with fluorescent chemo-affinity labeling using o-phthalaidehyde as the chemical initiator. Formation of isoindole derivative resulted in complete inactivation of the enzyme to hydrolyze both xylan and CMC as judged by fluorescence studies corroborating a single active site for the hydrolysis of xylan and CMC. (C) 2005 Elsevier Inc. All rights reserved.</p>},
	keywords = {Cellulase, CMC, OPTA, single active site, Thermomonospora sp., xylan, Xylanase},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2005.01.102},
	author = {Jagtap, Sharmili and Rao, M}
}
@article { ISI:000252096700006,
	title = {Biochemical characterization of a novel beta-1-3, 1-4 glucan 4-glucanohydrolase from thermomonospora sp having a single active site for lichenan and xylan},
	journal = {Biochimie},
	volume = {89},
	number = {12},
	year = {2007},
	month = {DEC},
	pages = {1489-1497},
	publisher = {ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER},
	type = {Article},
	address = {23 RUE LINOIS, 75724 PARIS, FRANCE},
	abstract = {<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>},
	keywords = {1-4 glucan 4-glucanohydrolase, beta-1-3, bifunctional, O-phthaialdehyde, single active site, Thermomonospora sp., Xylanase},
	issn = {0300-9084},
	doi = {10.1016/j.biochi.2007.06.010},
	author = {Anish, Ramakrishnan and Rao, Mala}
}
