1f6w: Difference between revisions

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==Overview==

Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a, variety of lipids in the small intestine. A distinct property of BAL is, its dependency on bile salts in hydrolyzing substrates of long acyl chains, or bulky alcoholic motifs. A crystal structure of the catalytic domain of, human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has, been determined at 2.3 A resolution. The crystal form belongs to space, group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein, shows an alpha/beta hydrolase fold. In the absence of bound bile salt, molecules, the protein possesses a preformed catalytic triad and a, functional oxyanion hole. Several surface loops around the active site are, mobile, including two loops potentially involved in substrate binding, (residues 115-125 and 270-285).

Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).

==Disease==

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[[Category: esterase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a, variety of lipids in the small intestine. A distinct property of BAL is, its dependency on bile salts in hydrolyzing substrates of long acyl chains, or bulky alcoholic motifs. A crystal structure of the catalytic domain of, human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has, been determined at 2.3 A resolution. The crystal form belongs to space, group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein, shows an alpha/beta hydrolase fold. In the absence of bound bile salt, molecules, the protein possesses a preformed catalytic triad and a, functional oxyanion hole. Several surface loops around the active site are, mobile, including two loops potentially involved in substrate binding, (residues 115-125 and 270-285).
+Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).
 ==Disease==
@@ Line 23: / Line 23: @@
 [[Category: esterase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:46:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:30 2008''