Evidence map›Paper›PMID 25038786›Full record

ArticleNature chemical biology2014

Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis.

Giang K T Nguyen, Shujing Wang, Yibo Qiu, Xinya Hemu, Yilong Lian, James P Tam

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Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.

0numbers the graph read from it
0cells of the map it votes in
180citing papers in PubMed
14.0field-weighted citation impact, top 1% of its field
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

180 citing papers in PubMed, 425 citations in OpenAlex.

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  19. Metabolite Mediated Protein Macrocyclization.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025
    Article
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120 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Giang K T NguyenSchool of Biological Sciences, Nanyang Technological University, Singapore.
Shujing WangSchool of Biological Sciences, Nanyang Technological University, Singapore.
Yibo QiuSchool of Biological Sciences, Nanyang Technological University, Singapore.
Xinya HemuSchool of Biological Sciences, Nanyang Technological University, Singapore.
Yilong LianSchool of Biological Sciences, Nanyang Technological University, Singapore.
James P TamSchool of Biological Sciences, Nanyang Technological University, Singapore.
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteases are ubiquitous in nature, whereas naturally occurring peptide ligases, enzymes catalyzing the reverse reactions of proteases, are rare occurrences. Here we describe the discovery of butelase 1, to our knowledge the first asparagine/aspartate (Asx) peptide ligase to be reported. This highly efficient enzyme was isolated from Clitoria ternatea, a cyclic peptide-producing medicinal plant. Butelase 1 shares 71% sequence identity and the same catalytic triad with legumain proteases but does not hydrolyze the protease substrate of legumain. Instead, butelase 1 cyclizes various peptides of plant and animal origin with yields greater than 95%. With Kcat values of up to 17 s(-1) and catalytic efficiencies as high as 542,000 M(-1) s(-1), butelase 1 is the fastest peptide ligase known. Notably, butelase 1 also displays broad specificity for the N-terminal amino acids of the peptide substrate, thus providing a new tool for C terminus-specific intermolecular peptide ligations.

Indexed as

Amino Acid SequenceAnimalsAsparagineAspartic AcidAspartic Acid EndopeptidasesClitoriaCyclizationDisulfidesHumansHydrolysisKineticsLigasesMacrocyclic CompoundsModels, MolecularMolecular Sequence DataPeptidesAsparagineAspartic AcidAspartic Acid EndopeptidasesDisulfidesLigasesMacrocyclic CompoundsPeptidesPeptide SynthasesPlant ProteinsRecombinant Proteins

Identifiers

PMID25038786
OpenAlexW2048797519

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.