Evidence map›Paper›PMID 22767596›Full record

ArticleThe Journal of biological chemistry2012

Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase.

Hirofumi Komori, Yoko Nitta, Hiroshi Ueno, Yoshiki Higuchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

  1. Pooled it
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  11. Review
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  13. Article
  14. Anti-Allergic Effects ofAntioxidants (Basel, Switzerland) · 2021
    Article
  15. Structural basis for substrate specificity of l-methionine decarboxylase.Protein science : a publication of the Protein Society · 2021
    Article
  16. Article
  17. Review
  18. Crystal structure ofJournal of advanced research · 2020
    Article
  19. Article
  20. Biocatalytic synthesis of α-amino ketones.Synlett : accounts and rapid communications in synthetic organic chemistry · 2019
    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

4 authors at 3 institutions in 1 country.

Hirofumi KomoriDepartment of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan. komori@sci.u-hyogo.ac.jp
Yoko Nitta
Hiroshi Ueno
Yoshiki Higuchi
University of Hyogo · JPNara Women's University · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histamine is an important chemical mediator for a wide variety of physiological reactions. L-histidine decarboxylase (HDC) is the primary enzyme responsible for histamine synthesis and produces histamine from histidine in a one-step reaction. In this study, we determined the crystal structure of human HDC (hHDC) complexed with the inhibitor histidine methyl ester. This structure shows the detailed features of the pyridoxal-5'-phosphate inhibitor adduct (external aldimine) at the active site of HDC. Moreover, a comparison of the structures of hHDC and aromatic L-amino acid (L-DOPA) decarboxylase showed that Ser-354 was a key residue for substrate specificity. The S354G mutation at the active site enlarged the size of the hHDC substrate-binding pocket and resulted in a decreased affinity for histidine, but an acquired ability to bind and act on L-DOPA as a substrate. These data provide insight into the molecular basis of substrate recognition among the group II pyridoxal-5'-phosphate-dependent decarboxylases.

Indexed as

Amino Acid SubstitutionBinding SitesHistidineHistidine DecarboxylaseHumansLevodopaMutation, MissensePhosphoric Monoester HydrolasesProtein Structure, TertiaryStructure-Activity RelationshipSubstrate SpecificityHistidineHistidine DecarboxylaseLevodopaPhosphoric Monoester Hydrolasespyridoxal-5-phosphatase

Identifiers

PMID22767596
PMCPMC3436558
OpenAlexW2138360609

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.