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

Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi.

Journal of bacteriology - 1 Apr 2003

Xu Ying, Feller Georges, Gerday Charles, Glansdorff Nicolas

Abstract excerpt

The enzyme ornithine carbamoyltransferase (OTCase) of Moritella abyssi (OTCase(Mab)), a new, strictly psychrophilic and piezophilic bacterial species, was purified. OTCase(Mab) displays maximal activity at rather low temperatures (23 to 25 degrees C) compared to other cold-active enzymes and is much less thermoresistant than its homologues from Escherichia coli or thermophilic procaryotes. In vitro the enzyme is...

Read the complete abstract on PubMed

Topics

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

Share to Adaptation, Biological
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cold Temperature

Share to Enzyme Stability

Share to Ornithine

Share to Ornithine Carbamoyltransferase

Share to Protein Structure, Quaternary

Share to Sequence Analysis

Source

Open in PubMed Open full text

Identifiers

PMID: 12644485
DOI: 10.1128/JB.185.7.2161-2168.2003
PMCID: PMC151491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi.PMID 12644485Read ↗

Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants.Semantic proximity Read ↗

Mechanistic and Crystallographic Studies of Azoreductase AzoA from Bacillus wakoensis A01.Semantic proximity Read ↗

Binuclear Metallohydrolases: Complex Mechanistic Strategies for a Simple Chemical ReactionSemantic proximity Read ↗

Activation mechanism and activity of globupain, a thermostable C11 protease from the Arctic Mid-Ocean Ridge hydrothermal systemSemantic proximity Read ↗

Biochemical characterization and mutational analysis of the tetrameric DABA transaminase EctB from the Arctic bacterium Marinobacter sp. CK1.Semantic proximity Read ↗

Structural and functional characterization of a cold-adapted stand-alone TPM domain reveals a relationship between dynamics and phosphatase activity.Semantic proximity Read ↗

Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme.Semantic proximity Read ↗

Characterization of a novel high-pH-tolerant laccase-like multicopper oxidase and its sequence diversity in Thioalkalivibrio sp.Semantic proximity Read ↗

Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability.Semantic proximity Read ↗

Low-temperature extremophiles and their applications.Semantic proximity Read ↗

Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.Semantic proximity Read ↗

Systematic screening for catalytic promiscuity in 4-oxalocrotonate tautomerase: enamine formation and aldolase activity.Semantic proximity Read ↗

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