@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:000239324300008,
	title = {Conformation and microenvironment of the active site of a low molecular weight 1,4-beta-D-glucan glucanohydrolase from an alkalothermophilic thermomonospora sp.: involvement of lysine and cysteine residues},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {347},
	number = {2},
	year = {2006},
	month = {AUG},
	pages = {428-432},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	type = {Article},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Conformation and microenvironment at the active site of 1,4-beta-D-glucan glucanohydrolase was probed with fluorescent chemo-affinity labeling using o-phthalaldehyde. OPTA has been known to form a fluorescent isoindole derivative by cross-linking the proximal thiol and amino groups of cysteine and lysine. Modification of lysine of the enzyme by TNBS and of cysteine residue by PHMB abolished the ability of the enzyme to form an isoindole derivative with OPTA. Kinetic analysis of the TNBS and PHMB-modified enzyme suggested the presence of essential lysine and cysteine residues, respectively, at the active site of the enzyme. The substrate protection of the enzyme with carboxymethylcellulose (CMC) confirmed the involvement of lysine and cysteine residues in the active site of the enzyme. Multiple sequence alignment of peptides obtained by tryptic digestion of the enzyme showed cysteine is one of the conserved amino acids corroborating the chemical modification studies. (c) 2006 Elsevier Inc. All rights reserved.</p>},
	keywords = {1, 4-beta-D-glucan glucanohydrolase, active site microenvironment, Cysteine, lysine, OPTA, PHMB, Thermomonospora sp., TNBS},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2006.06.100},
	author = {Jagtap, Sharmili and Rao, Mala}
}
