<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jogi, Shraddha</style></author><author><style face="normal" font="default" size="100%">Jagtap, Rutuja</style></author><author><style face="normal" font="default" size="100%">Subrahmanyam, Yalamanchili Venkata</style></author><author><style face="normal" font="default" size="100%">Sharma, Monika</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Mahesh</style></author><author><style face="normal" font="default" size="100%">Raghunathan, Anu</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Engineering pichia pastoris as a heterologous platform for non-ribosomal peptide biosynthesis of the β-lactam intermediate δ-(L-α-Aminoadipyl)-L-cysteinyl-D-valine (ACV)</style></title><secondary-title><style face="normal" font="default" size="100%">ACS Omega</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">11</style></volume><pages><style face="normal" font="default" size="100%">32038-32048</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	The production of nonribosomal peptides (NRPs) in non-native hosts remains challenging due to the size and complexity of the biosynthetic enzymes. Here, we report the first successful reconstruction of the delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) pathway in Pichia pastoris. By introducing codon-optimized versions of the pcbAB and npgA genes directly into the genome, we were able to rebuild the minimal pathway required for ACV synthesis, which we confirmed using LC-MS/MS. Although the starting strain produced only small amounts of ACV (similar to 5 ng/mL), yields increased 10-fold after adaptive evolution (similar to 50 ng/mL) and further improved with precursor supplementation (similar to 60 ng/mL). Transcriptomic analysis showed that the engineered strain reorganized its metabolism to meet the energy and precursor demands of NRPS activity. Overall, this study suggests that P. pastoris can serve as a practical, proof-of-concept host for complex NRP biosynthesis and lays the groundwork for future engineering of beta-lactam pathways.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">22</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	5.1&lt;/p&gt;
</style></custom4></record></records></xml>