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Titolo:
Crystal structure of the catalytic domain of human bile salt activated lipase
Autore:
Terzyan, S; Wang, CS; Downs, D; Hunter, B; Zhang, XC;
Indirizzi:
Oklahoma Med Res Fdn, Crystallog Program, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn Oklahoma City OK USA 73104 lahoma City, OK 73104 USA Oklahoma Med Res Fdn, Prot Studies Program, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn Oklahoma City OK USA 73104 lahoma City, OK 73104 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 9, volume: 9, anno: 2000,
pagine: 1783 - 1790
SICI:
0961-8368(200009)9:9<1783:CSOTCD>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC CHOLESTEROL ESTERASE; CANDIDA-RUGOSA LIPASE; HUMAN-MILK; DEPENDENT LIPASE; STIMULATED LIPASE; MOLECULAR-CLONING; PROTEIN; TOOL; CRYSTALLOGRAPHY; SUBSTRATE;
Keywords:
bile salt activated lipase; crystal structure; esterase; substrate specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Zhang, XC Oklahoma Med Res Fdn, Crystallog Program, 825 NE 13th St, Oklahoma City, OK 73104 USA Oklahoma Med Res Fdn 825 NE 13th St Oklahoma City OK USA 73104 A
Citazione:
S. Terzyan et al., "Crystal structure of the catalytic domain of human bile salt activated lipase", PROTEIN SCI, 9(9), 2000, pp. 1783-1790

Abstract

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 Angstrom 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).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/07/18 alle ore 13:40:12