02010nas a2200229   4500008004100000022001400041245011000055210006900165260007300234300001200307490000700319520113100326653004101457653001801498653002601516100001701542700001601559700002501575700002401600700002701624856012901651       2014                        eng d  a0141-813000aLeucaena sp recombinant cinnamyl alcohol dehydrogenase: purification and physicochemical characterization0 aLeucaena sp recombinant cinnamyl alcohol dehydrogenase purificat  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a254-2600 v633 a<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>10aCinnamyl alcohol dehydrogenase (CAD)10aMetalloenzyme10aSubstrate specificity1 aPatel, Parth1 aGupta, Neha1 aGaikwad, Sushama, M.1 aAgrawal, Dinesh, C.1 aKhan, Bashir, Mohammad  uhttps://library.ncl.res.in/content/leucaena-sp-recombinant-cinnamyl-alcohol-dehydrogenase-purification-and-physicochemical-0