@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}
}
