PXD056235-1

PXD056235 is an original dataset announced via ProteomeXchange.

Title	Biosynthesis of novel non-proteinogenic amino acids β-hydroxyenduracididine and β-methylphenylalanine in Escherichia coli
Description	Non-proteinogenic amino Q7 Q8 acids (npAAs) are valuable building blocks for the development of advanced pharmaceuticals and agrochemicals. The surge in interest in their synthesis is primarily due to the potential to enhance and diversify existing bioactive molecules. This can be achieved by altering these bioactive molecules to improve their effectiveness, reducing resistance compared to their natural counterparts or generating molecules with novel functions. Traditional production of npAAs in native hosts requires specialized conditions and complex cultivation media. Furthermore, these compounds are often found in organisms that challenge genetic manipulation. Thus, the recombinant production of these npAAs in a model organism like Escherichia coli paves the way for groundbreaking advancements in synthetic biology. For the first time, we report the synthesis of npAAs β-methylphenylalanine (BmePhe), β- hydroxyenduracididine (BhEnd), and enduracididine (End) from Streptomyces hygroscopicus in E. coli. Through proteomic and metabolomic analyses, we achieved the production of these compounds from two synthetic operons, comprising five heterologous proteins. Interestingly, we discovered that the exogenous addition of pathway precursors to the E. coli system enhanced the yield of BmePhe by 2.5 times, whereas it concurrently attenuated the production of BhEnd and End, signifying a selective precursor-dependent yield enhancement. The synthetic biology landscape is broadened in this study by expanding the repertoire of amino acids beyond the conventional set of 22 standard proteinogenic amino acids. The biosynthesized npAAs, End, BhEnd, and BmePhe hold promise for engineering proteins with modified functions, integrating into novel metabolites and/or enhancing biological stability and activity. Additionally, these amino acids’ biological production and subsequent purification present an alternative to traditional chemical synthesis methods, paving a direct pathway for pharmacological evaluation.
HostingRepository	PRIDE
AnnounceDate	2024-10-01
AnnouncementXML	Submission_2024-09-30_17:35:43.873.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rosemary Gillane
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Revision	Datetime	Status	ChangeLog Entry
0	2024-09-25 05:57:29	ID requested
⏵ 1	2024-09-30 17:35:44	announced
2	2024-10-22 07:00:11	announced	2024-10-22: Updated project metadata.

10.3389/FBIOE.2024.1468974;

submitter keyword: E. coli, heterologous expression, enduracididine,non-proteinogenic amino acids, Streptomyces, β-methylphenylalanine, β- hydroxyenduracididine

Esteban Marcellin
contact affiliation	AIBN, University of Queensland
contact email	e.marcellin@uq.edu.au
lab head
Rosemary Gillane
contact affiliation	University of Queensland
contact email	r.gillane@uq.edu.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD056235
     1. Label: PRIDE project
     2. Name: Biosynthesis of novel non-proteinogenic amino acids β-hydroxyenduracididine and β-methylphenylalanine in Escherichia coli