Evidence map›Paper›PMID 15358859›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning.

Hiroshi Fukatsu, Yoshiteru Hashimoto, Masahiko Goda, Hiroki Higashibata, Michihiko Kobayashi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Natural low-molecular mass organic compounds with oxidase activity as organocatalysts.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  5. Article
  6. Article
  7. Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  8. Novel isonitrile hydratase involved in isonitrile metabolism.The Journal of biological chemistry · 2010
    Article
  9. Article
  10. Article
  11. Discovery of a reaction intermediate of aliphatic aldoxime dehydratase involving heme as an active center.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

5 authors at 2 institutions in 1 country.

Hiroshi FukatsuInstitute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan.
Yoshiteru Hashimoto
Masahiko Goda
Hiroki Higashibata
Michihiko Kobayashi
University of Tsukuba · JPInstitute of Applied Biochemistry · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-substituted formamide was produced through the hydration of an isonitrile by isonitrile hydratase in the isonitrile metabolism. The former compound was further degraded by a microorganism, strain F164, which was isolated from soil through an acclimatization culture. The N-substituted formamide-degrading microorganism was identified as Arthrobacter pascens. The microbial degradation was found to proceed through an enzymatic reaction, the N-substituted formamide being hydrolyzed to yield the corresponding amine and formate. The enzyme, designated as N-substituted formamide deformylase (NfdA), was purified and characterized. The native enzyme had a molecular mass of approximately 61 kDa and consisted of two identical subunits. It stoichiometrically catalyzed the hydrolysis of N-benzylformamide (an N-substituted formamide) to benzylamine and formate. Of all of the N-substituted formamides tested, N-benzylformamide was the most suitable substrate for the enzyme. However, no amides were accepted as substrates. The gene (nfdA) encoding this enzyme was also cloned. The deduced amino acid sequence of nfdA exhibited the highest overall sequence identity (28%) with those of regulatory proteins among known proteins. Only the N-terminal region (residues 58-72) of NfdA also showed significant sequence identity (27-73%) to that of each member of the amidohydrolase superfamily, although there was no similarity in the overall sequence except in the above limited region.

Indexed as

AmidohydrolasesAminesAmino Acid SequenceChromatography, Ion ExchangeCloning, MolecularConserved SequenceKineticsMolecular Sequence DataMolecular WeightProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidAmidohydrolasesAminesN-substituted formamide deformylaseRecombinant Proteins

Identifiers

PMID15358859
PMCPMC518824
OpenAlexW2038572787

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.