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Titolo:
A MONO-FUNCTIONAL 3-DEOXY-D-MANNO-OCTULOSONIC ACID (KDO) TRANSFERASE AND A KDO KINASE IN EXTRACTS OF HAEMOPHILUS-INFLUENZAE
Autore:
WHITE KA; KALTASHOV IA; COTTER RJ; RAETZ CRH;
Indirizzi:
DUKE UNIV,MED CTR,DEPT BIOCHEM DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT BIOCHEM DURHAM NC 27710 JOHNS HOPKINS UNIV,DEPT PHARMACOL,MIDDLE ATLANTIC MASS SPECTROMETRY LAB BALTIMORE MD 21205
Titolo Testata:
The Journal of biological chemistry
fascicolo: 26, volume: 272, anno: 1997,
pagine: 16555 - 16563
SICI:
0021-9258(1997)272:26<16555:AM3A(T>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIPID-A MUTANTS; ESCHERICHIA-COLI; SALMONELLA-TYPHIMURIUM; 3-DEOXY-D-MANNOOCTULOSONATE-8-PHOSPHATE SYNTHETASE; LIPOPOLYSACCHARIDE BIOSYNTHESIS; BORDETELLA-PERTUSSIS; IDENTIFICATION; ENDOTOXINS; STRAIN; OLIGOSACCHARIDE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
K.A. White et al., "A MONO-FUNCTIONAL 3-DEOXY-D-MANNO-OCTULOSONIC ACID (KDO) TRANSFERASE AND A KDO KINASE IN EXTRACTS OF HAEMOPHILUS-INFLUENZAE", The Journal of biological chemistry, 272(26), 1997, pp. 16555-16563

Abstract

Lipopolysaccharide of Haemophilus influenzae contains a single 3-deoxy-D-manno-octulosonic acid (Kdo) residue, linked to the 6' position oflipid A. In Escherichia coli and related organisms, a Kdo disaccharide is attached to lipid A. In previous studies, we cloned the gene (kdtA) encoding the E. coli Kdo transferase and demonstrated that homogeneous preparations of KdtA polypeptide catalyzed the attachment of both Kdo groups to the precursor, lipid IVA. E. coli KdtA produced only traces of mono-glycosylated product. We now show that a single Kdo is transferred to lipid IVA in extracts of H. influenzae. The mono-functional Kdo transferase of H. influenzae is membrane-bound, and the reactionis dependent upon a CMP-Kdo-generating system, as in E. coli. The specific activity of Kdo transfer to lipid IVA is 0.5-1 nmol/min/mg in H.influenzae membranes. Utilizing solubilized H. influenzae membranes, milligram quantities of Kdo-lipid IVA were prepared for analysis. Matrix-assisted laser desorption/ionization mass spectrometry revealed a parent ion (M - H)(-) at m/z 1626.0, consistent with the addition of a single Kdo moiety. Like lipid IVA, Kdo-lipid IVA was an excellent substrate for the bi-functional Kdo transferase of E. coli. In membranes of H. influenzae, but not E. coli, Kdo-lipid IVA was further phosphorylated in the presence of ATP, yielding a mono-phosphorylated Kdo-lipid IVA with a parent ion (M - H)(-) at m/z 1703.9. The identification of the monofunctional H. influenzae Kdo transferase, which is encoded by a KdtA homologue that displays 50% identity to its E. coli counterpart, should facilitate the mechanistic dissection of more complex multi-functional Kdo transferases, like those of E. coli and Chlamydia trachomatis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 09:45:33