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Titolo:
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor
Autore:
Gutknecht, R; Beutler, R; Garcia-Alles, LF; Baumann, U; Erni, B;
Indirizzi:
Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland Univ Bern BernSwitzerland CH-3012 & Biochem, CH-3012 Bern, Switzerland
Titolo Testata:
EMBO JOURNAL
fascicolo: 10, volume: 20, anno: 2001,
pagine: 2480 - 2486
SICI:
0261-4189(20010515)20:10<2480:TDKOEC>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUGAR PHOSPHOTRANSFERASE SYSTEM; MANNOSE TRANSPORTER; ENZYME-I; SALMONELLA-TYPHIMURIUM; CATABOLITE CONTROL; CRYSTAL-STRUCTURE; PROTEIN; PHOSPHOENOLPYRUVATE; PERMEASE; SUBUNIT;
Keywords:
dihydroxyacetone kinase; phosphohistidine; protein phosphorylation; PTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Erni, B Univ Bern, Dept Chem & Biochem, Freie Str 3, CH-3012 Bern, Switzerland Univ Bern Freie Str 3 Bern Switzerland CH-3012 Bern, Switzerland
Citazione:
R. Gutknecht et al., "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor", EMBO J, 20(10), 2001, pp. 2480-2486

Abstract

The dihydroxyacetone kinase (DhaK) of Escherichia coli consists of three soluble protein subunits, DhaK (YcgT; 39.5 kDa) and DhaL (YcgS; 22.6 kDa) are similar to the N- and C-terminal halves of the ATP-dependent DhaK ubiquitous in bacteria, animals and plants. The homodimeric DhaM (YcgC; 51.6 kDa) consists of three domains. The N-terminal dimerization domain has the same fold as the IIA domain (PDB code 1PDO) of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS), The middle domain is similar to HPr and the C-terminus is similar to the N-terminaldomain of enzyme I (EI) of the PTS, DhaM is phosphorylated three times by phosphoenolpyruvate in an EI- and HPr-dependent reaction. DhaK and DhaL arenot phosphorylated, The IIA domain of DhaM, instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha), Unlike the carbohydrate-specific transporters of the PTS, DhaK, DhaL and DhaM have no transport activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 05:18:34