Implication of a tyrosine residue in the unspecific bile salt binding site of human pancreatic carboxylic ester hydrolase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference34 articles.
1. Modification of the essential amino acids of human pancreatic carboxylic-ester hydrolase
2. Catalytic properties of modified human pancreatic carboxylic-ester hydrolase
3. Binding of human pancreatic carboxylic ester hydrolase to lipid interfaces
4. Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters
5. On the Probable Involvement of Arginine Residues in the Bile-Salt-Binding Site of Human Pancreatic Carboxylic Ester Hydrolase
Cited by 17 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Nitration of tyrosine residues 368 and 345 in the β-subunit elicits FoF1-ATPase activity loss;Biochemical Journal;2009-09-25
2. Site-directed Mutagenesis of the Distal Basic Cluster of Pancreatic Bile Salt-dependent Lipase;Journal of Biological Chemistry;2004-09
3. Site-directed Mutagenesis of the Basic N-terminal Cluster of Pancreatic Bile Salt-dependent Lipase;Journal of Biological Chemistry;2002-09
4. Inhibition of yeast lipase (CRL1) and cholesterol esterase (CRL3) by 6-chloro-2-pyrones: comparison with porcine cholesterol esterase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2002-04
5. Importance of Arginines 63 and 423 in Modulating the Bile Salt-dependent and Bile Salt-independent Hydrolytic Activities of Rat Carboxyl Ester Lipase;Journal of Biological Chemistry;2000-08
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