Evidence map›Paper›PMID 19088069›Full record

ArticleThe Journal of biological chemistry2009

Mechanistic insights into the hydrolysis and synthesis of ceramide by neutral ceramidase.

Tsuyoshi Inoue, Nozomu Okino, Yoshimitsu Kakuta, Atsushi Hijikata, Hiroyuki Okano, Hatsumi M Goda, Motohiro Tani, Noriyuki Sueyoshi, Kouji Kambayashi, Hiroyoshi Matsumura and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. 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
0.8field-weighted citation impact, top 28% 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Catalytic Mechanism of Eukaryotic Neutral Ceramidase.Structure (London, England : 1993) · 2015
    Article
  10. Sphingosine-1-phosphate metabolism: A structural perspective.Critical reviews in biochemistry and molecular biology · 2015
    Review
  11. Article
  12. Review
  13. Article
  14. PLP-dependent enzymes as entry and exit gates of sphingolipid metabolism.Protein science : a publication of the Protein Society · 2011
    Review
  15. Article
  16. Article
  17. Review
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

12 authors at 4 institutions in 1 country.

Tsuyoshi InoueDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-Oka, Suita, Osaka 565-0871, Japan. inouet@chem.eng.osaka-u.ac.jp
Nozomu Okino
Yoshimitsu Kakuta
Atsushi Hijikata
Hiroyuki Okano
Hatsumi M Goda
Motohiro Tani
Noriyuki Sueyoshi
Kouji Kambayashi
Hiroyoshi Matsumura
Yasushi Kai
Makoto Ito
Kyushu University · JPOsaka University · JPJapan Science and Technology Agency · JPRIKEN Center for Integrative Medical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ceramidase (CDase; EC 3.5.1.23) hydrolyzes ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. The crystal structures of neutral CDase from Pseudomonas aeruginosa (PaCD) in the C2-ceramide-bound and -unbound forms were determined at 2.2 and 1.4 A resolutions, respectively. PaCD consists of two domains, and the Zn(2+)- and Mg(2+)/Ca(2+)-binding sites are found within the center of the N-terminal domain and the interface between the domains, respectively. The structural comparison between the C2-ceramide-bound and unbound forms revealed an open-closed conformational change occurring to loop I upon binding of C2-ceramide. In the closed state, this loop sits above the Zn(2+) coordination site and over the opening to the substrate binding site. Mutational analyses of residues surrounding the Zn(2+) of PaCD and rat neutral CDase revealed that the cleavage or creation of the N-acyl linkage of ceramide follows a similar mechanism as observed for the Zn(2+)-dependent carboxypeptidases. The results provide an understanding of the molecular mechanism of hydrolysis and synthesis of ceramide by the enzyme. Furthermore, insights into the actions of PaCD and eukaryotic neutral CDases as an exotoxin and mediators of sphingolipid signaling are also revealed, respectively.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalytic DomainCell LineCeramidesCrystallography, X-RayHumansHydrolysisMetalsModels, MolecularMolecular Sequence DataMutationNeutral CeramidaseProtein Structure, TertiaryPseudomonas aeruginosaCeramidesMetalsNeutral Ceramidase

Identifiers

PMID19088069
PMCPMC2666609
OpenAlexW2026231134

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.