Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190

Applied Microbiology and Biotechnology

Volumn 99, Issue 10, 2015, Pages 4297-4307

  Miyakawa, Takuya ^a   Mizushima, Hiroki ^a   Ohtsuka, Jun ^a   Oda, Masayuki ^b   Kawai, Fusako ^c   Tanokura, Masaru ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b KYOTO PREFECTURAL UNIVERSITY   (Japan)

^c KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

Ca2+ activation; Cutinase type polyesterase; PET hydrolase; Saccharomonospora viridis AHK190; Thermostability

Indexed keywords

CHEMICAL ACTIVATION; CONFORMATIONS; ENZYMATIC HYDROLYSIS; HYDROLASES; IONS; MOLECULES; PLASTIC BOTTLES; STABILITY;

CONFORMATIONAL CHANGE; CRYSTALLOGRAPHIC DATA; OPEN CONFORMATION; POLYESTERASE; POLYETHYLENE TEREPHTHALATES (PET); SACCHAROMONOSPORA VIRIDIS; THERMOSTABILITY; THERMOSTABILIZATION;

CALCIUM;

BACTERIAL PROTEIN; CALCIUM; CARBOXYLESTERASE; CUTINASE; POLYETHYLENE TEREPHTHALATE;

ACTINOMYCETALES; AMINO ACID SEQUENCE; BINDING SITE; BIOREMEDIATION; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

ACTINOMYCETALES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; BIODEGRADATION, ENVIRONMENTAL; CALCIUM; CARBOXYLIC ESTER HYDROLASES; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; POLYETHYLENE TEREPHTHALATES; SEQUENCE ALIGNMENT;

EID: 84939936734     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6272-8     Document Type: Article

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