Evidence map›Paper›PMID 19684168›Full record

ArticleApplied and environmental microbiology2009

Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli.

Shota Atsumi, Zhen Li, James C Liao

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

42 citing papers in PubMed, 107 citations in OpenAlex.

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  6. Engineering in life sciences · 2023
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  20. A synthetic pathway for the production of 2-hydroxyisovaleric acid in Escherichia coli.Journal of industrial microbiology & biotechnology · 2018
    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

3 authors at 1 institution in 1 country.

Shota AtsumiDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, California 90095, USA.
Zhen Li
James C Liao
University of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A pathway toward isobutanol production previously constructed in Escherichia coli involves 2-ketoacid decarboxylase (Kdc) from Lactococcus lactis that decarboxylates 2-ketoisovalerate (KIV) to isobutyraldehyde. Here, we showed that a strain lacking Kdc is still capable of producing isobutanol. We found that acetolactate synthase from Bacillus subtilis (AlsS), which originally catalyzes the condensation of two molecules of pyruvate to form 2-acetolactate, is able to catalyze the decarboxylation of KIV like Kdc both in vivo and in vitro. Mutational studies revealed that the replacement of Q487 with amino acids with small side chains (Ala, Ser, and Gly) diminished only the decarboxylase activity but maintained the synthase activity.

Indexed as

Acetolactate SynthaseAmino Acid SubstitutionBacillus subtilisButanolsCarboxy-LyasesEscherichia coliHemiterpenesKeto AcidsLactatesMutagenesis, Site-DirectedPyruvic AcidAcetolactate Synthasealpha-acetolactatealpha-ketoisovalerateButanolsCarboxy-LyasesHemiterpenesisobutyl alcoholKeto AcidsLactatesPyruvic Acid

Identifiers

PMID19684168
PMCPMC2753059
OpenAlexW2127399533

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.