Strzelczyk_2016_Acta.Biochim.Pol_63_103

Reference

Title : Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica - Strzelczyk_2016_Acta.Biochim.Pol_63_103
Author(s) : Strzelczyk P , Bujacz GD , Kielbasinski P , Blaszczyk J
Ref : Acta Biochim Pol , 63 :103 , 2016
Abstract :

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.

PubMedSearch : Strzelczyk_2016_Acta.Biochim.Pol_63_103
PubMedID: 26716135
Gene_locus related to this paper: canar-LipB

Related information

Gene_locus canar-LipB
Structure 4ZV7

Citations formats

Strzelczyk P, Bujacz GD, Kielbasinski P, Blaszczyk J (2016)
Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica
Acta Biochim Pol 63 :103

Strzelczyk P, Bujacz GD, Kielbasinski P, Blaszczyk J (2016)
Acta Biochim Pol 63 :103