Uppenberg_1994_Structure_2_293

Reference

Title : The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica - Uppenberg_1994_Structure_2_293
Author(s) : Uppenberg J , Hansen MT , Patkar S , Jones TA
Ref : Structure , 2 :293 , 1994
Abstract :

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 for lipase B from the yeast Candida antarctica. The primary sequence has no significant homology to any other known lipase and deviates from the consensus sequence around the active site serine that is found in other lipases. We have determined the crystal structure of this enzyme using multiple isomorphous replacement methods for two crystal forms. Models for the orthorhombic and monoclinic crystal forms of the enzyme have been refined to 1.55 A and 2.1 A resolution, respectively. Lipase B is an alpha/beta type protein that has many features in common with previously determined lipase structures and other related enzymes. In the monoclinic crystal form, lipid-like molecules, most likely beta-octyl glucoside, can be seen close to the active site. The behaviour of these lipid molecules in the crystal structure has been studied at different pH values. CONCLUSION: The structure of Candida antarctica lipase B shows that the enzyme has a Ser-His-Asp catalytic triad in its active site. The structure appears to be in an 'open' conformation with a rather restricted entrance to the active site. We believe that this accounts for the substrate specificity and high degree of stereospecificity of this lipase.

PubMedSearch : Uppenberg_1994_Structure_2_293
PubMedID: 8087556
Gene_locus related to this paper: canar-LipB

Related information

Substrate Octylglucoside
Gene_locus Octylglucoside    canar-LipB
Family Octylglucoside    canar-LipB    Canar_LipB    Lipase_3
Structure Octylglucoside    canar-LipB    Canar_LipB    Lipase_3    1TCA    1TCB    1TCC

Citations formats

Uppenberg J, Hansen MT, Patkar S, Jones TA (1994)
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
Structure 2 :293

Uppenberg J, Hansen MT, Patkar S, Jones TA (1994)
Structure 2 :293