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

Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.

Chemistry & biology - 1 Apr 2008

Sachdeva Sarbjot, Musayev Faik N, Alhamadsheh Mamoun M, Scarsdale J Neel, Wright H Tonie, Reynolds Kevin A

Abstract excerpt

Mycobacterium tuberculosis FabH initiates type II fatty acid synthase-catalyzed formation of the long chain (C(16)-C(22)) acyl-coenzyme A (CoA) precursors of mycolic acids, which are major constituents of the bacterial cell envelope. Crystal structures of M. tuberculosis FabH (mtFabH) show the su...

Read the complete abstract on PubMed

Topics

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

Share to Acyl Coenzyme A
Share to Catalytic Domain
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Inhibitors

Share to Hydrophobic and Hydrophilic Interactions

Share to Mycolic Acids

Share to Solvents

Share to Spectrometry, Mass, Electrospray Ionization

Source

Identifiers

PMID: 18420147
DOI: 10.1016/j.chembiol.2008.03.007

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18420147-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.PMID 18420147Read ↗

Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity.Semantic proximity Read ↗

Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.Semantic proximity Read ↗

The tail of mycolic acids.Semantic proximity Read ↗

Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Semantic proximity Read ↗

Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis.Semantic proximity Read ↗

A universal pocket in fatty acyl-AMP ligases ensures redirection of fatty acid pool away from coenzyme A-based activation.Semantic proximity Read ↗

HadD, a novel fatty acid synthase type II protein, is essential for alpha- and epoxy-mycolic acid biosynthesis and mycobacterial fitnessSemantic proximity Read ↗

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.Semantic proximity Read ↗

Substrate recognition by β-ketoacyl-ACP synthases.Semantic proximity Read ↗

Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.Semantic proximity Read ↗

A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites.Semantic proximity Read ↗

Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II.Semantic proximity Read ↗

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