Enzymatic hydrolysis of PET: functional roles of three Ca2+ ions bound to a cutinase-like enzyme, Cut190*, and its engineering for improved activity
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DOI: 10.1007/s00253-018-9374-x
Abstract: Cut190 from Saccharomonospora viridis AHK190 (Cut190) is the only cutinase that exhibits inactive (Ca2+-free) and active (Ca2+-bound) states, although other homologous cutinases always maintain the active states (Ca2+-free and bound). The X-ray crystallography of the… read more here.
Keywords: ions bound; three ca2; ca2 free; ca2 ... See more keywords
Folding thermodynamics of PET-hydrolyzing enzyme Cut190 depending on Ca2+ concentration
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DOI: 10.1007/s10973-018-7447-9
Abstract: The enzyme, cutinase from Saccharomonospora viridis AHK190 (Cut190), can hydrolyze the inner block of polyethylene terephthalate (PET). Cut190 has a unique feature that both its activity and thermal stability are increased upon Ca2+ binding. In… read more here.
Keywords: ca2 concentration; thermodynamics; folding thermodynamics; cut190 ... See more keywords
Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from Saccharomonospora viridis AHK190 in Substrate-Bound States Elucidates the Ca2+-Driven Catalytic Cycle.
Sign Up to like & getrecommendations! Published in 2018 at "Biochemistry"
DOI: 10.1021/acs.biochem.8b00624
Abstract: A cutinase-type polyesterase from Saccharomonospora viridis AHK190 (Cut190) has been shown to degrade the inner block of polyethylene terephthalate. A unique feature of Cut190 is that its function and stability are regulated by Ca2+ binding.… read more here.
Keywords: cutinase; form; viridis ahk190; saccharomonospora viridis ... See more keywords