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Titolo:
CHARACTERIZATION OF SFP, A BACILLUS-SUBTILIS PHOSPHOPANTETHEINYL TRANSFERASE FOR PEPTIDYL CARRIER PROTEIN DOMAINS IN PEPTIDE SYNTHETASES
Autore:
QUADRI LEN; WEINREB PH; LEI M; NAKANO MM; ZUBER P; WALSH CT;
Indirizzi:
HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOL PHARMACOL BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOL PHARMACOL BOSTON MA 02115 LOUISIANA STATE UNIV,MED CTR,DEPT BIOCHEM & MOL BIOL SHREVEPORT LA 71130
Titolo Testata:
Biochemistry
fascicolo: 6, volume: 37, anno: 1998,
pagine: 1585 - 1595
SICI:
0006-2960(1998)37:6<1585:COSABP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEHYDROGENASE MULTIENZYME COMPLEX; SURFACTIN PRODUCTION; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; NUCLEOTIDE-SEQUENCE; RATIONAL DESIGN; LIPOYL DOMAIN; BIOSYNTHESIS; GENE; COMPETENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
L.E.N. Quadri et al., "CHARACTERIZATION OF SFP, A BACILLUS-SUBTILIS PHOSPHOPANTETHEINYL TRANSFERASE FOR PEPTIDYL CARRIER PROTEIN DOMAINS IN PEPTIDE SYNTHETASES", Biochemistry, 37(6), 1998, pp. 1585-1595

Abstract

The Bacillus subtilis enzyme Sfp, required for production of the lipoheptapeptide antibiotic surfactin, posttranslationally phosphopantetheinylates a serine residue in each of the seven peptidyl carrier protein domains of the first three subunits (SrfABC) of surfactin synthetaseto yield docking sites for amino acid loading and peptide bond formation. With recombinant Sfp and 16-17-kDa peptidyl carrier protein (PCP)domains excised from the SrfB1 and SrfB2 modules as apo substrates, k(cat) values of 56-104 min(-1) and K-m values of 1.3-1.8 mu M were determined, indicating equivalent recognition of the adjacent PCP domainsby Sfp. In contrast to other phosphopantetheinyl transferases (PPTases) previously examined, Sfp will modify the apo forms of heterologous recombinant proteins, including the PCP domain of Saccharomyces cerevisiae Lys2 (involved in lysine biosynthesis), the aryl carrier protein (ArCP) domain of Escherichia coli EntB (involved in enterobactin biosynthesis), and the E. coli acyl carrier protein (ACP) subunit, suggesting Sfp as a good candidate for heterologous coexpression with peptide and polyketide synthase genes to overproduce holo-synthase enzymes. Cosubstrate coenzyme A (CoA), the phosphopantetheinyl group donor, has aK-m of 0.7 mu M. Desulfo-CoA and homocysteamine-CoA are also substrates of Sfp, and benzoyl-CoA and phenylacetyl-CoA are also utilized by Sfp, resulting in direct transfer of acyl phosphopantetheinyl moieties into the carrier protein substrate. Mutagenesis in Sfp of five residues conserved across the PPTase family was assessed for in vivo effects on surfactin production and in vitro effects on PPTase activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 04:30:37