@article { ISI:000296937200031,
	title = {Jack bean alpha-mannosidase (Jb alpha-man): tolerance to alkali, chelating and reducing agents and energetics of catalysis and inhibition},
	journal = {International Journal of Biological Macromolecules},
	volume = {49},
	number = {5},
	year = {2011},
	month = {DEC},
	pages = {1066-1071},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Investigations of the catalytic and structural transitions of jack bean alpha-mannosidase (Jb alpha-man) are described in the present paper. The enzyme was maximally stable at pH 5.0; however, when incubated in the pH range of 11.0-12.0, showed 1.3 times higher activity and also stability for longer time. The free amino group at or near the active site was probably involved in the stability and activation mechanism. The active site is constituted by the association of two unidentical subunits connected by disulfide linkages. The metalloenzyme has Zn(2+) ions tightly bound and chelation reduces the thermal stability of the protein. Energetics of catalysis and thermodynamics of inhibition of the enzyme were also carried out. (C) 2011 Elsevier B.V. All rights reserved.</p>},
	keywords = {Alkali tolerance, alpha-Mannosidase, beta-Mercaptoethanol, Energetics, Inhibition, Metalloenzyme},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2011.08.033},
	author = {Kumar, Avinash and Gaikwad, Sushama M.}
}
@article { ISI:000330603800038,
	title = {Leucaena sp recombinant cinnamyl alcohol dehydrogenase: purification and physicochemical characterization},
	journal = {International Journal of Biological Macromolecules},
	volume = {63},
	year = {2014},
	month = {FEB},
	pages = {254-260},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Cinnamyl alcohol dehydrogenase is a broad substrate specificity enzyme catalyzing the final step in monolignol biosynthesis, leading to lignin formation in plants. Here, we report characterization of a recombinant CAD homologue (LICAD2) isolated from Leucaena leucocephala. LICAD2 is 80 kDa homodimer associated with non-covalent interactions, having substrate preference toward sinapaldehyde with K-cat/K-m of 11.6 x 10(6) (M-1 s(-1)), and a possible involvement of histidine at the active site. The enzyme remains stable up to 40 C, with the deactivation rate constant (K-d*) and half-life (t(1/2)) of 0.002 and 5 h, respectively. LICAD2 showed optimal activity at pH 6.5 and 9 for reduction and oxidation reactions, respectively, and was stable between pH 7 and 9, with the deactivation rate constant (K-d*) and half-life (t(1/2)) of 7.5 x 10(-4) and 15 h, respectively. It is a Zn-metalloenzyme with 4 Zn2+ per dimer, however, was inhibited in presence of externally supplemented Zn2+ ions. The enzyme was resistant to osmolytes, reducing agents and non-ionic detergents. (C) 2013 Elsevier B.V. All rights reserved.</p>},
	keywords = {Cinnamyl alcohol dehydrogenase (CAD), Metalloenzyme, Substrate specificity},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2013.09.005},
	author = {Patel, Parth and Gupta, Neha and Gaikwad, Sushama M. and Agrawal, Dinesh C. and Khan, Bashir Mohammad}
}
