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

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.

Nature chemical biology - 1 Feb 2008

Kaplun Alexander, Binshtein Elad, Vyazmensky Maria, Steinmetz Andrea, Barak Ze'ev, Chipman David M, Tittmann Kai, Shaanan Boaz

Abstract excerpt

Thiamine diphosphate (ThDP), a derivative of vitamin B1, is an enzymatic cofactor whose special chemical properties allow it to play critical mechanistic roles in a number of essential metabolic enzymes. It has been assumed that all ThDP-dependent enzymes exploit a polar interaction between a strictly conserved glutamate and the N1' of the ThDP moiety. The crystal structure of glyoxylate carboligase challenges...

Read the complete abstract on PubMed

Topics

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

Share to Carboxy-Lyases
Share to Carboxylic Acids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Glutamates

Share to Phosphates

Share to Thiamine

Share to Thiazoles

Share to Valine

Source

Identifiers

PMID: 18176558
DOI: 10.1038/nchembio.62

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.PMID 18176558Read ↗

Significant catalytic roles for Glu47 and Gln 110 in all four of the C-C bond-making and -breaking steps of the reactions of acetohydroxyacid synthase II.Semantic proximity Read ↗

Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes.Semantic proximity Read ↗

Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases.Semantic proximity Read ↗

Theoretical Studies of the Electronic Absorption Spectra of Thiamin Diphosphate in Pyruvate Decarboxylase.Semantic proximity Read ↗

Competence of Thiamin Diphosphate-Dependent Enzymes with 2'-Methoxythiamin Diphosphate Derived from Bacimethrin, a Naturally Occurring Thiamin Anti-vitamin.Semantic proximity Read ↗

Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.Semantic proximity Read ↗

Characterization of Cg10062 from Corynebacterium glutamicum: implications for the evolution of cis-3-chloroacrylic acid dehalogenase activity in the tautomerase superfamily.Semantic proximity Read ↗

Aminomutases: mechanistic diversity, biotechnological applications and future perspectives.Semantic proximity Read ↗

A molecular switch and proton wire synchronize the active sites in thiamine enzymes.Semantic proximity Read ↗

Stand-alone lipoylated H-protein of the glycine cleavage system enables glycine cleavage and the synthesis of glycine from one-carbon compounds <i>in vitro</i>Semantic proximity Read ↗

Probing the function of a ligand-modulated dynamic tunnel in bifunctional proline utilization A (PutA).Semantic proximity Read ↗

Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.Semantic proximity Read ↗

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