Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
نویسندگان
چکیده
During crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.
منابع مشابه
Intermediate Production of Mono- and Diolein by an Immobilized Lipase from Candida antarctica
Lipase from Candida antarctica, fixed on macroporous acrylic resin, has been used for the intermediate production of mono- and diolein by hydrolysis of triolein. The effect of altering concentrations of triolein and glycerol and the function of the molecular sieve on the hydrolysis reaction of triolein were investigated. The highest hydrolysis yield was observed for the utmost concentration of ...
متن کاملThe sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica.
BACKGROUND Lipases constitute a family of enzymes that hydrolyze triglycerides. They occur in many organisms and display a wide variety of substrate specificities. In recent years, much progress has been made towards explaining the mechanism of these enzymes and their ability to hydrolyze their substrates at an oil-water interface. RESULTS We have determined the DNA and amino acid sequences f...
متن کاملA novel self-activation mechanism of Candida antarctica lipase B.
Candida antarctica lipase B (CalB), resembling many other lipases structure-wise, contains a flexible lid that undergoes a surprisingly large conformational change when catalyzing hydrophobic substrates (e.g. triglycerides). Despite extensive and important applications in industry, it is so far still elusive whether CalB can be activated on a hydrophobic surface, like other lipases. From large-...
متن کاملResidue-specific global fluorination of Candida antarctica lipase B in Pichia pastoris.
We report the in vivo fluorination of the tryptophan, tyrosine, and phenylalanine residues in a glycosylation-deficient mutant of Candida antarctica lipase B, CalB N74D, expressed in the methylotrophic yeast Pichia pastoris and subsequently segregated into the growth medium. To achieve this, a P. pastoris strain auxotrophic for all three aromatic amino acids was supplemented with 5-fluoro-L-try...
متن کاملFunctional Motions of Candida antarctica Lipase B: A Survey through Open-Close Conformations
Candida antarctica lipase B (CALB) belongs to psychrophilic lipases which hydrolyze carboxyl ester bonds at low temperatures. There have been some features reported about cold-activity of the enzyme through experimental methods, whereas there is no detailed information on its mechanism of action at molecular level. Herein, a comparative molecular dynamics simulation and essential dynamics analy...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Acta biochimica Polonica
دوره 63 1 شماره
صفحات -
تاریخ انتشار 2016