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Titolo:
STRUCTURE AND MECHANISM OF A PROLINE-SPECIFIC AMINOPEPTIDASE FROM ESCHERICHIA-COLI
Autore:
WILCE MCJ; BOND CS; DIXON NE; FREEMAN HC; GUSS JM; LILLEY PE; WILCE JA;
Indirizzi:
UNIV SYDNEY,DEPT BIOCHEM,BLDG G08 SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA AUSTRALIAN NATL UNIV,RES SCH CHEM CANBERRA ACT 0200 AUSTRALIA
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 95, anno: 1998,
pagine: 3472 - 3477
SICI:
0027-8424(1998)95:7<3472:SAMOAP>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
METHIONINE AMINOPEPTIDASE; CREATINE AMIDINOHYDROLASE; PROTEIN MODELS; PROLIDASE; REFINEMENT; INHIBITION; PEPTIDES; SEQUENCE; ARGINASE; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
M.C.J. Wilce et al., "STRUCTURE AND MECHANISM OF A PROLINE-SPECIFIC AMINOPEPTIDASE FROM ESCHERICHIA-COLI", Proceedings of the National Academy of Sciences of the United Statesof America, 95(7), 1998, pp. 3472-3477

Abstract

The structure of the praline-specific amino-peptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-Angstrom resolution, for a dipeptide inhibited complex at 2.3-Angstrom resolution, and for a low-pH inactive form at 2.7-Angstrom resolution, The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that theprotein is a tetramer under physiological conditions, The monomer folds into two domains, The active site, in the larger C-terminal domain,contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro, The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits, The fold of the proteinresembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 08:11:37