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Titolo:
Increasing the thermal stability of euphauserase - A cold-active and multifunctional serine protease from Antarctic krill
Autore:
Benjamin, DC; Kristjansdottir, S; Gudmundsdottir, A;
Indirizzi:
Univ Iceland, Inst Sci, Dept Food Sci, IS-101 Reykjavik, Iceland Univ Iceland Reykjavik Iceland IS-101 ood Sci, IS-101 Reykjavik, Iceland Univ Virginia, Sch Med, Dept Microbiol, Charlottesville, VA 22908 USA UnivVirginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 1, volume: 268, anno: 2001,
pagine: 127 - 131
SICI:
0014-2956(200101)268:1<127:ITTSOE>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
COD GADUS-MORHUA; ATLANTIC COD; CONFORMATIONAL SEARCH; CHYMOTRYPSIN; RECOGNITION; PROTEINASE; MOLECULES; CLEAVAGE; COMPLEX;
Keywords:
brachyurin; mutations; serine protease; similarity modeling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Gudmundsdottir, A Univ Iceland, Inst Sci, Dept Food Sci, Vatnsmyrarvegi 16, IS-101 Reykjavik, Iceland Univ Iceland Vatnsmyrarvegi 16 Reykjavik Iceland IS-101
Citazione:
D.C. Benjamin et al., "Increasing the thermal stability of euphauserase - A cold-active and multifunctional serine protease from Antarctic krill", EUR J BIOCH, 268(1), 2001, pp. 127-131

Abstract

A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold-active and thermally sensitive enzyme with a high affinity for Lys, Arg and large hydrophobic amino acids. Residue Phe137 in euphauserase, localized in loop D (autolysis loop), is highly exposed on the surface of the molecule. Therefore, it appeared to be an easy target for autolysis. The broadly specific euphauserase has a low affinity for negatively charged residues. Inorder to increase the stability of the enzyme, two mutants were created inwhich residue Phe137 was replaced by a Glu and an Asp residue. Both mutations resulted in increased stability of the recombinant euphauserase towardsthermal inactivation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 01:09:13