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Titolo:
Catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase
Autore:
Baasov, T; Tkacz, R; Sheffer-Dee-Noor, S; Belakhov, V;
Indirizzi:
Technion Israel Inst Technol, Dept Chem, IL-32000 Haifa, Israel Technion Israel Inst Technol Haifa Israel IL-32000 L-32000 Haifa, Israel Technion Israel Inst Technol, Inst Catalysis Sci & Technol, IL-32000 Haifa, Israel Technion Israel Inst Technol Haifa Israel IL-32000 L-32000 Haifa, Israel
Titolo Testata:
CURRENT ORGANIC CHEMISTRY
fascicolo: 2, volume: 5, anno: 2001,
pagine: 127 - 138
SICI:
1385-2728(200102)5:2<127:CMO3S>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PUTATIVE REACTION INTERMEDIATE; 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE SYNTHETASE; ENZYME KDO8P SYNTHASE; ESCHERICHIA-COLI; TETRAHEDRAL INTERMEDIATE; EPSP SYNTHASE; ACID KDO; LIPOPOLYSACCHARIDE BIOSYNTHESIS; STRUCTURAL ELUCIDATION; 3-DEOXY-D-ARABINO-HEPTULOSONIC ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
68
Recensione:
Indirizzi per estratti:
Indirizzo: Baasov, T Technion Israel Inst Technol, Dept Chem, IL-32000 Haifa, Israel Technion Israel Inst Technol Haifa Israel IL-32000 ifa, Israel
Citazione:
T. Baasov et al., "Catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase", CURR ORG CH, 5(2), 2001, pp. 127-138

Abstract

Catalytic mechanism of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthase (EC 4.1.2.16), an enzyme involved in the biosynthesis of lipopolysaccharides of Gram-negative bacteria, remains a Fascinating subject for both bioorganic and medicinal researches. The enzyme catalyzes an aldol-type condensation of D-arabinose 5-phosphate with phosphoenolpyruvate to produce the unusual eight-carbon saccharide KDO8P and inorganic phosphate. The structure and mechanism of KDO8P synthase have actively studied during last decade as this enzyme represents an important target for antibiotic therapy. This review summarizes the most mechanistically relevant information reported to date, with special emphases on the synthesis and evaluation of a number of analogues of substrates, product and proposed intermediates of the KDO8P-synthase-catalyzed reaction. The results introduced here illustrate the value of organic synthesis to characterize enzymatic reaction. Mechanistic postulates have pointed the way to the design of potent inhibitors, and these in turn have provided insight into details of the reaction, as well as useful structural models for elusive intermediates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 15:03:02