Evidence map›Paper›PMID 39475147›Full record

ArticleBiochemistry2024

Crystal Structure and Mutagenesis of an XYP Subfamily Cyclodipeptide Synthase Reveal Key Determinants of Enzyme Activity and Substrate Specificity.

Jun-Bin He, Yichen Ren, Peifeng Li, Yi-Pei Liu, Hai-Xue Pan, Lin-Juan Huang, Jiayuan Wang, Pengfei Fang, Gong-Li Tang

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Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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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

9 authors.

Jun-Bin HeState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.
Yichen RenState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.
Peifeng LiState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.
Yi-Pei LiuShaanxi Natural Carbohydrate Resource Engineering Research Center, College of Food Science and Technology, Northwest University, Xi'an 710069, China.
Hai-Xue PanState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.
Lin-Juan HuangShaanxi Natural Carbohydrate Resource Engineering Research Center, College of Food Science and Technology, Northwest University, Xi'an 710069, China.
Jiayuan WangState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.
Pengfei FangState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.ORCID 0000-0002-3448-5494
Gong-Li TangState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences (CAS), Shanghai 200032, China.ORCID 0000-0003-3149-4683

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclodipeptide synthases (CDPSs) catalyze the synthesis of diverse cyclodipeptides (CDPs) by utilizing two aminoacyl-tRNA (aa-tRNA) substrates in a sequential ping-pong reaction mechanism. Numerous CDPSs have been characterized to provide precursors for diketopiperazines (DKPs) with diverse structural characteristics and biological activities. BcmA, belonging to the XYP subfamily, is a cyclo(l-Ile-l-Leu)-synthesizing CDPS involved in the biosynthesis of the antibiotic bicyclomycin. The structural basis and determinants influencing BcmA enzyme activity and substrate selectivity are not well understood. Here, we report the crystal structure of

Indexed as

Mutagenesis, Site-DirectedPeptide SynthasesStreptomycesAmino Acid SequenceBacterial ProteinsCatalytic DomainCrystallography, X-RayModels, MolecularProtein ConformationSubstrate SpecificityBacterial ProteinsPeptide Synthases

Identifiers

PMID39475147
PMCPMC11580168

What OpenQuestion holds

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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.