Discovery and development of penicillin-binding protein-type thioesterases as biocatalysts.

Zachary L Budimir, Elizabeth I Parkinson

Abstract readReview

In one paragraph

Review in Current opinion in biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Zachary L BudimirJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.

Elizabeth I ParkinsonJames Tarpo Jr. and Margaret Tarpo Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA; Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA. Electronic address: eparkins@purdue.edu.

Funding

Mining Cryptic Biosynthetic Gene Clusters for Novel Bioactive Compounds and BiocatalystsR35GM138002 · NIGMS · PURDUE UNIVERSITY · PI Elizabeth Ivy Parkinson · 2020 to 2026

$2.9M

NIGMS NIH HHS R35 GM138002

6 · The paper itself

Abstract

Cyclic peptides are promising drug candidates, but their synthesis, especially the synthesis of small, strained rings, remains challenging. Penicillin-binding protein-type thioesterases (PBP-TEs) have emerged as versatile biocatalysts that catalyze head-to-tail macrocyclization of nonribosomal peptides. Unlike canonical thioesterase domains, which catalyze diverse offloading outcomes, PBP-TEs exclusively promote head-to-tail cyclization, offering predictable reactivity. Their ability to act on diverse substrates in vitro further underscores their potential as tools for peptide drug discovery. This review highlights PBP-TE discovery and substrate scope investigation, along with recent advances in structural characterization and engineering, establishing these enzymes as a promising platform for the biocatalytic synthesis of cyclic peptides.

Indexed as

Penicillin-Binding ProteinsPeptides, CyclicThiolester HydrolasesBiocatalysisDrug DiscoveryProtein EngineeringPenicillin-Binding ProteinsPeptides, CyclicThiolester Hydrolases

Identifiers

PMID41435497

DOI10.1016/j.copbio.2025.103417

PMCPMC12786034

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.