AbstractThe crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation was determined at 1.5Å resolution. This structure highly resembles that of Serratia marcescens LipA in an open conformation, except for the structures of two lids. Lid1 is anchored by a Ca2+ ion (Ca1) in an open conformation, but lacks this Ca1 site and greatly changes its structure and position in a closed conformation. Lid2 forms a helical hairpin in an open conformation, but does not form it and covers the active site in a closed conformation. Based on these results, we discuss on the lid-opening mechanism
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
AbstractBackground: The interfacial activation of lipases results primarily from conformational chan...
AbstractThe crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conforma...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Å res...
AbstractBackground: The interfacial activation of lipases results primarily from conformational chan...
AbstractWe report the 1.7 Å resolution crystal structure of the Lip2 lipase from Yarrowia lipolytica...
AbstractBackground: Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are...
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open con...
AbstractThe family of lipases (triacylglycerol-acyl-hydrolases, EC 3.1.1.3) constitutes an interesti...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Angst...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Angst...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25–45uC...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
AbstractBackground: The interfacial activation of lipases results primarily from conformational chan...
AbstractThe crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conforma...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Å res...
AbstractBackground: The interfacial activation of lipases results primarily from conformational chan...
AbstractWe report the 1.7 Å resolution crystal structure of the Lip2 lipase from Yarrowia lipolytica...
AbstractBackground: Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are...
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open con...
AbstractThe family of lipases (triacylglycerol-acyl-hydrolases, EC 3.1.1.3) constitutes an interesti...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Angst...
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Angst...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25–45uC...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C...
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
In nature, lipases (EC 3.1.1.3) catalyze the hydrolysis of triglycerides to form glycerol and fatty ...
AbstractBackground: The interfacial activation of lipases results primarily from conformational chan...