Evidence map›Paper›PMID 25862219›Full record

ArticleApplied and environmental microbiology2015

Utilization of D-Lactate as an Energy Source Supports the Growth of Gluconobacter oxydans.

Binbin Sheng, Jing Xu, Yingxin Zhang, Tianyi Jiang, Sisi Deng, Jian Kong, Chao Gao, Cuiqing Ma, Ping Xu

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Current Advances on Nanomaterials Interfering with Lactate Metabolism for Tumor Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
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 at 3 institutions in 1 country.

Binbin ShengState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Jing XuState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Yingxin ZhangState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Tianyi JiangState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Sisi DengState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Jian KongState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Chao GaoState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China jieerbu@sdu.edu.cn.
Cuiqing MaState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Ping XuState Key Laboratory of Microbial Metabolism and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, People's Republic of China.
Shandong University · CNState Key Laboratory of Microbial TechnologyShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

d-Lactate was identified as one of the few available organic acids that supported the growth of Gluconobacter oxydans 621H in this study. Interestingly, the strain used d-lactate as an energy source but not as a carbon source, unlike other lactate-utilizing bacteria. The enzymatic basis for the growth of G. oxydans 621H on d-lactate was therefore investigated. Although two putative NAD-independent d-lactate dehydrogenases, GOX1253 and GOX2071, were capable of oxidizing d-lactate, GOX1253 was the only enzyme able to support the d-lactate-driven growth of the strain. GOX1253 was characterized as a membrane-bound dehydrogenase with high activity toward d-lactate, while GOX2071 was characterized as a soluble oxidase with broad substrate specificity toward d-2-hydroxy acids. The latter used molecular oxygen as a direct electron acceptor, a feature that has not been reported previously in d-lactate-oxidizing enzymes. This study not only clarifies the mechanism for the growth of G. oxydans on d-lactate, but also provides new insights for applications of the important industrial microbe and the novel d-lactate oxidase.

Indexed as

BiocatalysisEnergy MetabolismGene DeletionGenetic Complementation TestGluconobacter oxydansKineticsLactate DehydrogenasesLactic AcidMixed Function OxygenasesOxidoreductasesOxygenSubstrate Specificitylactate 2-monooxygenaseLactate DehydrogenasesLactic AcidMixed Function OxygenasesOxidoreductasesOxygen

Identifiers

PMID25862219
PMCPMC4524133
OpenAlexW2021979788

What OpenQuestion holds

Textmetadata
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.