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

Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity.

PloS one - 1 Jan 2020

Baba Misato, Kojima Kenji, Nishimura Takuto, Sugiura Takuya, Takita Teisuke, Uehara Ryo, Crouch Robert J, Yasukawa Kiyoshi

Abstract excerpt

Ribonuclease H2 (RNase H2) exhibits both single ribonucleotide excision activity (activity A) and RNA strand degrading activity (activity B). Val143 of human RNase H2 is located at the active site and is conserved in eukaryotic RNase H2. In this study, we explored the role of Val143 in catalytic activity and substrate specificity. Nineteen single variants at amino acid position 143 were expressed in E. coli, and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Models, Molecular

Share to Mutation

Share to Ribonuclease H

Share to Substrate Specificity

Share to Valine

Source

Open in PubMed Open full text

Identifiers

PMID: 32069311
DOI: 10.1371/journal.pone.0228774
PMCID: PMC7028304

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Val143 of human ribonuclease H2 is not critical for, but plays a role in determining catalytic activity and substrate specificity.PMID 32069311Read ↗

Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II.Semantic proximity Read ↗

The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutières syndrome defects.Semantic proximity Read ↗

Residues Arg703, Asp777, and Arg781 of the RNase H domain of hepatitis B virus polymerase are critical for viral DNA synthesis.Semantic proximity Read ↗

The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity.Semantic proximity Read ↗

The conserved Lys-95 charged residue cluster is critical for the homodimerization and enzyme activity of human ribonucleotide reductase small subunit M2.Semantic proximity Read ↗

Ribonuclease H: from discovery to 3D structure.Semantic proximity Read ↗

Remarkable stabilization of a psychrotrophic RNase HI by a combination of thermostabilizing mutations identified by the suppressor mutation method.Semantic proximity Read ↗

High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation.Semantic proximity Read ↗

Hyperactivity of Human DNase I VariantsSemantic proximity Read ↗

Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition.Semantic proximity Read ↗

Construction and characterization of ribonuclease H2 C subunit-knockout NIH3T3 cells.Semantic proximity Read ↗

Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate.Semantic proximity Read ↗

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