Evidence map›Paper›PMID 29124361›Full record

ArticleExtremophiles : life under extreme conditions2018

Involvement of C-terminal amino acids of a hyperthermophilic serine racemase in its thermostability.

Masahito Murakami, Makoto Saito, Hirokazu Yokobori, Katsushi Nishimura, Minoru Tanigawa, Yoko Nagata

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Article in Extremophiles : life under extreme conditions, 2018. 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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0citing papers in PubMed
–field-weighted citation impact, top 87% of its field
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

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0 citing papers in PubMed, 1 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Masahito MurakamiDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan.
Makoto SaitoDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan.
Hirokazu YokoboriDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan.
Katsushi NishimuraDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan.
Minoru TanigawaDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan.
Yoko NagataDepartment of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Chiyoda-Ward, Tokyo, 101-8308, Japan. ocean_nagata@axel.ocn.ne.jp.
Nihon University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyrobaculum islandicum is a hyperthermophilic archaeon that grows optimally at 95-100 °C. In the previous study, we extensively purified a serine racemase from this organism and cloned the gene for overexpression in Escherichia coli (Ohnishi et al. 2008). This enzyme also exhibits highly thermostable L-serine/L-threonine dehydratase activity. In the present study, we aimed to elucidate the molecular mechanisms underlying the high thermostability of this enzyme. A recombinant variant of this enzyme, PiSRvt, constructed by truncating the C-terminal 72 amino acids, was compared with the native enzyme, PiSR. The dehydratase activity of PiSR and PiSRvt was found to owe to a homotrimer and a monomer, respectively, that demonstrated high and moderate thermostability, respectively. These observations reveal that the C-terminal region contributes to monomer trimerization that provides the extreme thermostability.

Indexed as

ThermotoleranceArchaeal ProteinsEnzyme StabilityProtein DenaturationProtein DomainsPyrobaculumRacemases and EpimerasesSerine RacemaseArchaeal ProteinsRacemases and EpimerasesSerine RacemaseArchaeaHyperthermophilesSerine racemaseSite-directed mutagenesisThermostabilityThreonine dehydratase

Identifiers

PMID29124361
OpenAlexW2767339554

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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.