Evidence map›Paper›PMID 15466039›Full record

ArticleJournal of bacteriology2004

Thermophilic, reversible gamma-resorcylate decarboxylase from Rhizobium sp. strain MTP-10005: purification, molecular characterization, and expression.

Masahiro Yoshida, Nobuhiro Fukuhara, Tadao Oikawa

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  6. Pressurized COGreen chemistry : an international journal and green chemistry resource : GC · 2018
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  9. Article
  10. Article
  11. Regioselective Enzymatic β-Carboxylation ofAdvanced synthesis & catalysis · 2015
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Crystallization and preliminary X-ray diffraction studies of maleylacetate reductase from Rhizobium sp. strain MTP-10005.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  17. 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 2 institutions in 1 country.

Masahiro YoshidaDepartment of Biotechnology, Faculty of Engineering, Kansai University, Suita, Osaka-Fu 564-8680, Japan.
Nobuhiro Fukuhara
Tadao Oikawa
Kansai University · JPMitsui Chemicals (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We found the occurrence of thermophilic reversible gamma-resorcylate decarboxylase (gamma-RDC) in the cell extract of a bacterium isolated from natural water, Rhizobium sp. strain MTP-10005, and purified the enzyme to homogeneity. The molecular mass of the enzyme was determined to be about 151 kDa by gel filtration, and that of the subunit was 37.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; in other words, the enzyme was a homotetramer. The enzyme was induced specifically by the addition of gamma-resorcylate to the medium. The enzyme required no coenzyme and did not act on 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 2-hydroxybenzoate, or 3-hydroxybenzoate. It was relatively thermostable to heat treatment, and its half-life at 50 degrees C was estimated to be 122 min; furthermore, it catalyzed the reverse carboxylation of resorcinol. The values of k(cat)/K(m) (mMu(-1) . s(-1)) for gamma-resorcylate and resorcinol at 30 degrees C and pH 7 were 13.4 and 0.098, respectively. The enzyme contains 327 amino acid residues, and sequence identities were found with those of hypothetical protein AGR C 4595p from Agrobacterium tumefaciens strain C58 (96% identity), 5-carboxyvanillate decarboxylase from Sphingomonas paucimobilis (32%), and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylases from Bacillus cereus ATCC 10987 (26%), Rattus norvegicus (26%), and Homo sapiens (25%). The genes (graA [1,230 bp], graB [888 bp], and graC [1,056 bp]) that are homologous to those in the resorcinol pathway also exist upstream and downstream of the gamma-RDC gene. Judging from these results, the resorcinol pathway also exists in Rhizobium sp. strain MTP-10005, and gamma-RDC probably catalyzes a reaction just before the hydroxylase in it does.

Indexed as

Carboxy-LyasesHot TemperatureAmino Acid SequenceAnimalsCloning, MolecularDNA, RibosomalEnzyme StabilityHumansHydroxybenzoatesMolecular Sequence DataPhylogenyRatsRhizobiumRNA, Ribosomal, 16SSequence AlignmentSequence Analysis, DNACarboxy-LyasesDNA, Ribosomalgamma-resorcylic acidHydroxybenzoatesRNA, Ribosomal, 16S

Identifiers

PMID15466039
PMCPMC522189
OpenAlexW2108234199

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.