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Titolo:
Cysteine-25 of adenylate kinase reacts with dithiothreitol to form an adduct upon aging of the enzyme
Autore:
Li, X; Han, Y; Pan, XM;
Indirizzi:
Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples RChina Acad Sinica Beijing Peoples R China 100101 eijing 100101, Peoples RChina
Titolo Testata:
FEBS LETTERS
fascicolo: 2, volume: 507, anno: 2001,
pagine: 169 - 173
SICI:
0014-5793(20011026)507:2<169:COAKRW>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADENOSINE-TRIPHOSPHATE TRANSPHOSPHORYLASES; HEMOLYTIC-ANEMIA; CRYSTALLINE RABBIT; CALF MUSCLE; DEFICIENCY; ERYTHROCYTE; MECHANISM; SUBSTITUTION;
Keywords:
protein aging; multiple native form; disulfide bridge; dithiothreitol adduct; conformation interconversion; rate-limiting step;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Pan, XM Acad Sinica, Inst Biophys, Natl Lab Biomacromol, 15 Datun Rd, Beijing 100101, Peoples R China Acad Sinica 15 Datun Rd Beijing Peoples R China 100101 es R China
Citazione:
X. Li et al., "Cysteine-25 of adenylate kinase reacts with dithiothreitol to form an adduct upon aging of the enzyme", FEBS LETTER, 507(2), 2001, pp. 169-173

Abstract

Adenylate kinase (AK) ages in solution in the presence Of DL-dithiothreitol (DTT) with a gradual activity decrease. Upon dilution with 4 M guanidine hydrochloride denatured native and aged AK, both recover to the same activity as the fresh enzyme. Mass spectroscopy and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole chloride modification kinetics studies identify that the residue cysteine-25 of the enzyme reacts with DTT to form an adduct. The formation of the unusual bridging DTT adduct of AK appears to be the result of a stable DTT-protein complex. The K-M for AMP, ADP and MgATP of the DTT-modified enzyme does not differ significantly from that of the intact enzyme, whereas the secondary and tertiary structures of the enzyme change obviously. These results indicate that cysteine-25 may not be involved directly in substrate binding, but may play an important role in maintaining secondary and tertiary structures of native AK, as well as the conformation interconversionin the catalytic cycle. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 19:04:32