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Titolo:
Coupling of proteolysis to ATP hydrolysis upon Escherichia coli Lon-protease functioning: II. Hydrolysis of ATP and activity of the enzyme peptide hydrolase sites
Autore:
Melnikov, EE; Tsirulnikov, KB; Rotanova, TV;
Indirizzi:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997,Russia Russian Acad Sci Moscow Russia 117997 ioorgan Chem, Moscow 117997,Russia
Titolo Testata:
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
fascicolo: 2, volume: 27, anno: 2001,
pagine: 101 - 109
SICI:
1068-1620(200103/04)27:2<101:COPTAH>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING SITES; LA; SUBSTRATE; FORMS; DEGRADATION; BREAKDOWN; PROTEINS; DOMAINS; MUTANT; RCSA;
Keywords:
ATPase; ATP-dependent proteolysis; E. coli; Lon protease; lon gene;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Rotanova, TV Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Ul Miklukho Maklaya 16-10,GSP-7, Moscow 117997, Russia Russian Acad Sci Ul Miklukho Maklaya 16-10,GSP-7 Moscow Russia 117997
Citazione:
E.E. Mel'nikov et al., "Coupling of proteolysis to ATP hydrolysis upon Escherichia coli Lon-protease functioning: II. Hydrolysis of ATP and activity of the enzyme peptide hydrolase sites", RUS J BIOOR, 27(2), 2001, pp. 101-109

Abstract

The absence of direct correlation between the efficiency of functioning ofATPase and peptide hydrolase sites of Lon protease was revealed. It was shown that Lon protease is an allosteric enzyme, in which the catalytic activity of peptide hydrolase sites is provided by the binding of nucleotides, their magnesium complexes, and free magnesium ions in the enzyme ATPase sites. It was revealed that the ADP-Mg complex, an inhibitor of the native enzyme, is an activator of the Lon-K362Q (the Lon protease mutant in the ATPasesite). Variants of functional contacts between different sites of the enzyme are considered. It was established that two ways of signal transduction from the ATPase sites to peptide hydrolase ones exist in the Lon protease oligomer-intra- and intersubunit ways. The enzyme ATPase sites are suggestedto be located in the areas of the complementary surfaces of subunits. It is hypothesized that upon degradation of protein substrates by the E. coli Lon protease in vivo ATP hydrolysis acts as a factor of limitation of the enzyme degrading activity.

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Documento generato il 20/01/20 alle ore 07:29:40