Evidence map›Paper›PMID 26573329›Full record

ArticleScientific reports2015

Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase.

Yoshio Kusakabe, Masaaki Ishihara, Tomonobu Umeda, Daisuke Kuroda, Masayuki Nakanishi, Yukio Kitade, Hiroaki Gouda, Kazuo T Nakamura, Nobutada Tanaka

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Biomolecules · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Homocysteine Attack on Vascular Endothelium-Old and New Features.International journal of molecular sciences · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Frontiers in cellular and infection microbiology · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Functional and Pathological Roles of AHCY.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. Biomolecules · 2020
    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

9 authors at 3 institutions in 1 country.

Yoshio KusakabeSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Masaaki IshiharaSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Tomonobu UmedaSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Daisuke KurodaSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Masayuki NakanishiCollege of Pharmaceutical Sciences, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama, Ehime 790-8578, Japan.
Yukio KitadeFaculty of Engineering, Gifu University, 1-1 Yanagido, Gifu, Gifu 501-1193, Japan.
Hiroaki GoudaSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Kazuo T NakamuraSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Nobutada TanakaSchool of Pharmacy, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Showa University · JPGifu University · JPMatsuyama University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-adenosyl-L-homocysteine hydrolase (SAH hydrolase or SAHH) is a highly conserved enzyme that catalyses the reversible hydrolysis of SAH to L-homocysteine (HCY) and adenosine (ADO). High-resolution crystal structures have been reported for bacterial and plant SAHHs, but not mammalian SAHHs. Here, we report the first high-resolution crystal structure of mammalian SAHH (mouse SAHH) in complex with a reaction product (ADO) and with two reaction intermediate analogues-3'-keto-aristeromycin (3KA) and noraristeromycin (NRN)-at resolutions of 1.55, 1.55, and 1.65 Å. Each of the three structures constitutes a structural snapshot of one of the last three steps of the five-step process of SAH hydrolysis by SAHH. In the NRN complex, a water molecule, which is an essential substrate for ADO formation, is structurally identified for the first time as the candidate donor in a Michael addition by SAHH to the 3'-keto-4',5'-didehydroadenosine reaction intermediate. The presence of the water molecule is consistent with the reaction mechanism proposed by Palmer &Abeles in 1979. These results provide insights into the reaction mechanism of the SAHH enzyme.

Indexed as

AdenosineAdenosylhomocysteinaseAmino Acid SequenceAnimalsBinding SitesBiocatalysisCrystallography, X-RayHydrolysisMiceMolecular Dynamics SimulationMolecular Sequence DataProtein Structure, TertiaryS-AdenosylhomocysteineSequence AlignmentSubstrate SpecificityAdenosineAdenosylhomocysteinasearisteromycinS-Adenosylhomocysteine

Identifiers

PMID26573329
PMCPMC4647836
OpenAlexW2411539690

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.