Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics.

Biochemistry - 22 Jan 2008

Rutherford Karen, Parson W W, Daggett Valerie

Abstract excerpt

Histamine N-methyltransferase (HNMT) is the primary enzyme responsible for inactivating histamine in the mammalian brain. The human HNMT gene contains a common threonine-isoleucine polymorphism at residue 105, distal from the active site. The 105I variant has decreased activity and lower protein...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Computer Simulation
Share to Histamine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to S-Adenosylmethionine

Source

Open in PubMed Open full text

Identifiers

PMID: 18154359
DOI: 10.1021/bi701737f
PMCID: PMC2905460

Genes

HNMT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18154359-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics.PMID 18154359Read ↗

Theoretical 3D model of histamine N-methyltransferase: insights into the effects of a genetic polymorphism on enzymatic activity and thermal stability.Semantic proximity Read ↗

The 108M polymorph of human catechol O-methyltransferase is prone to deformation at physiological temperatures.Semantic proximity Read ↗

Human histamine N-methyltransferase pharmacogenetics: common genetic polymorphisms that alter activity.Semantic proximity Read ↗

Four human thiopurine s-methyltransferase alleles severely affect protein structure and dynamics.Semantic proximity Read ↗

Effects of single nucleotide polymorphisms on human N-acetyltransferase 2 structure and dynamics by molecular dynamics simulation.Semantic proximity Read ↗

Histamine N-methyltransferase 939A>G polymorphism affects mRNA stability in patients with acetylsalicylic acid-intolerant chronic urticaria.Semantic proximity Read ↗

Histamine N-methyltransferase Thr105Ile is not associated with Parkinson's disease or essential tremor.Semantic proximity Read ↗

Molecular dynamics simulations reveal the impact of NUDT15 R139C and R139H variants in structural conformation and dynamics.Semantic proximity Read ↗

The Thr105Ile Variant (rs11558538) of the Histamine N-methyltransferase Gene may be associated with Reduced Risk of Parkinson Disease: A Meta-analysis.Semantic proximity Read ↗

No association between histamine N-methyltransferase functional polymorphism Thr105Ile and Alzheimer's disease.Semantic proximity Read ↗

Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol O-methyltransferase reaction.Semantic proximity Read ↗

Molecular dynamics simulations reveal the impact of NUTD15 variants in structural conformation and dynamicsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.