Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76Å resolution

Effect of hydrolysis products on the enzymatic degradation of polyethylene terephthalate nanoparticles by a polyester hydrolase from Thermobifida fusca

“…In a previous study, EG has been shown to inhibit the hydrolysis of the model ester p-nitrophenyl butyrate by the polyester hydrolase Est119 from Thermobifida alba, an enzyme homologous to TfCut2 [44]. However, the binding site of EG in Est119 was assumed not to be directly involved in the ester bond hydrolysis [45].…”

Synthetic Polyester-Hydrolyzing Enzymes From Thermophilic Actinomycetes

“…No unequivocal evidence has been provided regarding a metal ion requirement for the activity of the enzymes from T. fusca strains Hegde & Veeranki, 2013) or for LC-cutinase (Sulaiman et al, 2012). However, no structural component responsible for metal ion binding has been identified in the crystal structure of Est119 resolved at 1.76 Å (Kitadokoro et al, 2012). A dependence on up to 500 mM Ca 2+ ions has been clearly demonstrated for Est119 hydrolytic activity using pNPB and poly (butylene succinate-co-adipate) (PBSA) as substrates, as well as for its thermal stability at 50 C for an incubation period of up to 16 h .…”

“…Recently, the crystal structure of the metagenome-derived LC-cutinase was reported at a resolution of 1.5 Å (PDB ID: 4EB0; Sulaiman, You, Eiko, Koga, & Kanaya, 2013). The crystal structures of Est119 (Kitadokoro et al, 2012), LC-cutinase (Sulaiman et al, 2013), and TfCut2 (Roth et al, 2014) revealed a typical α/β hydrolase fold (Carr & Ollis, 2009;Ollis et al, 1992). The crystal structures of Est119 (Kitadokoro et al, 2012), LC-cutinase (Sulaiman et al, 2013), and TfCut2 (Roth et al, 2014) revealed a typical α/β hydrolase fold (Carr & Ollis, 2009;Ollis et al, 1992).…”

“…7.1A). The correspondent region in the structure of Est119 was described as two separate helices α7 and α8 (Kitadokoro et al, 2012). The short α1 helix of the LC-cutinase is a 3 10 helix (Fig.…”

Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

“…Therefore, the isolation of novel cutinases that possess special properties is of great potential economic value and importance. Cutinases are mainly found in different species of fungi (Castro-Ochoa et al, 2012;Fraga, Carvalho, & Macedo, 2012;Nyyssölä et al, 2014;Pio & Macedo, 2007;Roussel et al, 2014;Speranza & Macedo, 2013), although several bacterial cutinolytic enzymes have also been reported (Dutta, Krishnamoorthy, & Dasu, 2013;Hegde & Veeranki, 2013;Kitadokoro et al, 2012). A number of cutinases have been purified and characterized from various fungi, including Alternaria brassicicola (Koschorreck, Liu, Kazenwadel, Schmid, & Hauer, 2010), Coprinopsis cinerea (Merz, Schembecker, Riemer, Nimtz, & Zorn, 2009), Fusarium oxysporum (Fraga et al, 2012;Speranza & Macedo, 2013), Fusarium solani (Kwon, Kim, Yang, Song, & Song, 2009), Monilinia fructicola (Wang, Michailides, Hammock, Lee, & Bostock, 2002), Sirococcus conigenus , Trichoderma harzianum (Rubio, Cardoza, Hermosa, Gutierrez, & Monte, 2008) and Trichoderma reesei (Roussel et al, 2014).…”