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

Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.

The Journal of biological chemistry - 17 Feb 2017

Waz Shaimaa, Nakamura Teruya, Hirata Keisuke, Koga-Ogawa Yukari, Chirifu Mami, Arimori Takao, Tamada Taro, Ikemizu Shinji, Nakabeppu Yusaku, Yamagata Yuriko

Abstract excerpt

The human MutT homolog 1 (hMTH1, human NUDT1) hydrolyzes oxidatively damaged nucleoside triphosphates and is the main enzyme responsible for nucleotide sanitization. hMTH1 recently has received attention as an anticancer target because hMTH1 blockade leads to accumulation of oxidized nucleotides in the cell, resulting in mutations and death of cancer cells. Unlike Escherichia coli MutT, which shows high substrate...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to DNA Repair Enzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutation

Share to Phosphoric Monoester Hydrolases

Share to Protein Conformation

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 28035004
DOI: 10.1074/jbc.M116.749713
PMCID: PMC5314174

Genes

NUDT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.PMID 28035004Read ↗

Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates.Semantic proximity Read ↗

Structural Comparison of Enterococcus faecalis and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational VariabilitiesSemantic proximity Read ↗

Structural basis for substrate recognition by the human N-terminal methyltransferase 1.Semantic proximity Read ↗

Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.Semantic proximity Read ↗

A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides.Semantic proximity Read ↗

Structural Insights into the Mechanism of Base Excision by MBD4.Semantic proximity Read ↗

Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.Semantic proximity Read ↗

Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus.Semantic proximity Read ↗

Crystal structures of NUDT15 variants enabled by a potent inhibitor reveal the structural basis for thiopurine sensitivity.Semantic proximity Read ↗

Role of NUDIX Hydrolases in NAD and ADP-Ribose Metabolism in MammalsSemantic proximity Read ↗

Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?Semantic proximity Read ↗

Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.Semantic proximity Read ↗

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