DptA begins with a condensation (C) domain, whereasDptD ends with a thioesterase (Te) domain (Fig. 3e).Between these, domains for activation of specific aminoacids (A-domains), attachment to the NRPS by a panthethienyl tether (T-domains) and C-domains were foundin the expected number and order to comprise a total of13 modules, one for incorporation of each amino acid.Domains responsible for epimerization (E-domains) inmodules 8 and 11 for D-Ala and D-Ser, respectively, wereexpected given the reported activation of L- but not D-formsof Ala and Ser in biochemical studies (Wessels et al., 1996).An additional E-domain in module 2 (Fig. 3a, Table 2)was inconsistent with the published stereochemistry ofA21978C lipopeptides (Debono et al., 1987); this observation implied the presence of D-Asn instead of L-Asn inposition 2.
DptA begins with a condensation (C) domain, whereasDptD ends with a thioesterase (Te) domain (Fig. 3e).Between these, domains for activation of specific aminoacids (A-domains), attachment to the NRPS by a panthethienyl tether (T-domains) and C-domains were foundin the expected number and order to comprise a total of13 modules, one for incorporation of each amino acid.Domains responsible for epimerization (E-domains) inmodules 8 and 11 for D-Ala and D-Ser, respectively, wereexpected given the reported activation of L- but not D-formsof Ala and Ser in biochemical studies (Wessels et al., 1996).An additional E-domain in module 2 (Fig. 3a, Table 2)was inconsistent with the published stereochemistry ofA21978C lipopeptides (Debono et al., 1987); this observation implied the presence of D-Asn instead of L-Asn inposition 2.<br>
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