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

Probing the structural plasticity of an archaeal primordial cobaltochelatase CbiX(S).

Protein engineering, design & selection : PEDS - 1 Jun 2007

Pisarchik Alexander, Petri Ralf, Schmidt-Dannert Claudia

Abstract excerpt

Insertion of metal ions into tetrapyrrole macrocycles is catalyzed by a diverse group of enzymes called chelatases. Structures are known for several chelatases catalyzing metal insertion into protoporphyrin IX or sirohydrochlorin. Despite a lack of significant amino acid sequence similarity, these ferro- and cobaltochelatases share a high degree of structural similarity. Cobaltochelatase CbiK and ferrochelatase...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Bacterial Proteins
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Evolution, Molecular

Share to Ferrochelatase

Share to Lyases

Share to Models, Molecular

Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 17584754
DOI: 10.1093/protein/gzm018

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

Probing the structural plasticity of an archaeal primordial cobaltochelatase CbiX(S).PMID 17584754Read ↗

Identification of a Novel Cobamide Remodeling Enzyme in the Beneficial Human Gut Bacterium Akkermansia muciniphilaSemantic proximity Read ↗

Two distinct roles for two functional cobaltochelatases (CbiK) in Desulfovibrio vulgaris hildenborough.Semantic proximity Read ↗

Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrinSemantic proximity Read ↗

Identification and characterization of the 'missing' terminal enzyme for siroheme biosynthesis in α-proteobacteria.Semantic proximity Read ↗

Surveying the expanding prokaryotic Rubisco multiverse.Semantic proximity Read ↗

An evolutionary path to altered cofactor specificity in a metalloenzyme.Semantic proximity Read ↗

Tracking the evolution of porphobilinogen synthase metal dependence in vitro.Semantic proximity Read ↗

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.Semantic proximity Read ↗

An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase.Semantic proximity Read ↗

Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis.Semantic proximity Read ↗

Repurposed and artificial heme enzymes for cyclopropanation reactions.Semantic proximity Read ↗

A robust protein host for anchoring chelating ligands and organocatalysts.Semantic proximity Read ↗

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