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

Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3.

Applied and environmental microbiology - 1 Feb 2001

Ishikawa K, Ishida H, Matsui I, Kawarabayasi Y, Kikuchi H

Abstract excerpt

Genome sequencing of the thermophilic archaeon Pyrococcus horikoshii OT3 revealed a gene which had high sequence similarity to the gene encoding the carboxypeptidase of Sulfolobus solfataricus and also to that encoding the aminoacylase from Bacillus stearothermophilus. The gene from P. horikoshii comprises an open reading frame of 1,164 bp with an ATG initiation codon and a TGA termination codon, encoding a...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Carboxypeptidases
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hot Temperature

Share to Metals

Share to Multienzyme Complexes

Share to Recombinant Proteins

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 11157230
DOI: 10.1128/AEM.67.2.673-679.2001
PMCID: PMC92634

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3.PMID 11157230Read ↗

Functional similarities of a thermostable protein-disulfide oxidoreductase identified in the archaeon Pyrococcus horikoshii to bacterial DsbA enzymes.Semantic proximity Read ↗

Functional and structural characterization of thermostable D-amino acid aminotransferases from Geobacillus spp.Semantic proximity Read ↗

Exploring mutable conserved sites and fatal non-conserved sites by random mutation of esterase from Sulfolobus tokodaii and subtilisin from Thermococcus kodakarensis.Semantic proximity Read ↗

Enhancing the thermostability of transglutaminase from Streptomyces mobaraensis based on the rational design of a disulfide bond.Semantic proximity Read ↗

Active site of deblocking aminopeptidase from Pyrococcus horikoshii.Semantic proximity Read ↗

Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose.Semantic proximity Read ↗

Construction, expression, purification, characterization, and structural analysis of microbial transglutaminase variants.Semantic proximity Read ↗

A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus.Semantic proximity Read ↗

Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion.Semantic proximity Read ↗

Identification of the amino acid residues essential for proteolytic activity in an archaeal signal peptide peptidase.Semantic proximity Read ↗

Biochemical characterization and mutational improvement of a thermophilic esterase from Sulfolobus solfataricus P2.Semantic proximity Read ↗

Approaching transglutaminase from Streptomyces bacteria over three decadesSemantic proximity Read ↗

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