Converting Escherichia coli isochorismatase YecD into γ-lactamase.

Xiaoyan Guo, Yijie Tang, Xutao Zhao, Sheng Wu, Jianjun Wang

Abstract read

In one paragraph

Article in Bioresources and bioprocessing, 2025. 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

5 authors.

Xiaoyan GuoCollege of New Materials and Chemical Engineering, Beijing Institute of Petrochemical Technology, Beijing, 102617, People's Republic of China.

Yijie TangCollege of New Materials and Chemical Engineering, Beijing Institute of Petrochemical Technology, Beijing, 102617, People's Republic of China.

Xutao ZhaoCollege of New Materials and Chemical Engineering, Beijing Institute of Petrochemical Technology, Beijing, 102617, People's Republic of China.

Sheng WuCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, People's Republic of China.

Jianjun WangCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, People's Republic of China. wangjj@im.ac.cn.ORCID http://orcid.org/0000-0001-8205-7753

Funding

Beijing Municipal Commission of Education KM202110017009

6 · The paper itself

Abstract

Five Escherichia coli proteins in the isochorismatase superfamily (EntB, RutB, Nic, YcaC, and YecD) were cloned and expressed. Among them, only RutB exhibited ( +) γ-lactamase activity. The primary structures of these five proteins were compared to those of a ( +) γ-lactamase (Mhpg) from Microbacterium hydrocarbonoxydans. Subsequently, the active site constellations (ASCs) of the proteins were superimposed. By imitating the ASCs of Mhpg and RutB, a single mutation converted YecD into an active ( +) γ-lactamase (YecD-G145C). A mutant with three mutations (YecD-G145C-W115E-V67I) engineered through combinatorial saturation mutagenesis was created. The catalytic efficiency (k

Indexed as

Active site constellationIsochorismatasePromiscuity( +) γ-lactamase

Identifiers

PMID41137877

DOI10.1186/s40643-025-00960-y

PMCPMC12553813

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.