Pregled bibliografske jedinice broj: 51379
Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide (NRPS) synthetases (NRPS)
Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide (NRPS) synthetases (NRPS) // FEBS Letters, 498 (2001), 42-45 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 51379 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide (NRPS) synthetases (NRPS)
(Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide (NRPS))
Autori
Dieckmann, Ralf ; Neuhof, Torsten ; Pavela-Vrančič, Maja ; von Döhren, Hans
Izvornik
FEBS Letters (0014-5793) 498
(2001);
42-45
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Peptide synthetase; tyrocidine synthetase 1; adenylation domain; dipeptide generation.
Sažetak
A deletion mutant of tyrocidine synthetase 1 (&#916 ; &#916 ; TY1), comprising the adenylation domain of TY1 as an independent functional adenylate-forming unit, was used to investigate the ability of the adenylation domain to catalyse peptide bond formation from the aminoacyl adenylate intermediate. The results demonstrate that only one substrate amino acid needs to be activated as an aminoacyl adenylate. In view of the potential exploitation of peptide synthetases for enzymatic synthesis of dipeptides of choice, it is important to note that this does not necessarily require a dimodular construct or an intermediate acyl transfer step.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
177050
Ustanove:
Prirodoslovno-matematički fakultet, Split
Profili:
Maja Pavela-Vrančić
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- SCI-EXP, SSCI i/ili A&HCI