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

A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1.

Proceedings of the National Academy of Sciences of the United States of America - 7 Apr 2009

Widhalm Joshua R, van Oostende Chloë, Furt Fabienne, Basset Gilles J C

Abstract excerpt

Phylloquinone (vitamin K(1)) is a bipartite molecule that consists of a naphthoquinone ring attached to a phytyl side chain. The coupling of these 2 moieties depends on the hydrolysis of the CoA thioester of 1,4-dihydroxy-2-naphthoate (DHNA), which forms the naphthalenoid backbone. It is not known whether such a hydrolysis is enzymatic or chemical. In this study, comparative genomic analyses identified...

Read the complete abstract on PubMed

Topics

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

Share to Cyanobacteria
Share to Hydrolysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Metabolic Networks and Pathways

Share to Mutation

Share to Naphthols

Share to Naphthoquinones

Share to Substrate Specificity

Share to Thiolester Hydrolases

Source

Open in PubMed Open full text

Identifiers

PMID: 19321747
DOI: 10.1073/pnas.0900738106
PMCID: PMC2660889

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

A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1.PMID 19321747Read ↗

Phylloquinone (vitamin K(1) ) biosynthesis in plants: two peroxisomal thioesterases of Lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl-CoA.Semantic proximity Read ↗

Vitamin K1 (Phylloquinone): Function, Enzymes and GenesSemantic proximity Read ↗

Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. pcc 6803.Semantic proximity Read ↗

Current knowledge and recent advances in understanding metabolism of the model cyanobacterium Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Modification of topA in Synechococcus sp. PCC 7942 resulted in mutants capable of growing under low but not high concentration of CO2.Semantic proximity Read ↗

Gene expression under low-oxygen conditions in the cyanobacterium Synechocystis sp. PCC 6803 demonstrates Hik31-dependent and -independent responses.Semantic proximity Read ↗

The gene sml0013 of Synechocystis species strain PCC 6803 encodes for a novel subunit of the NAD(P)H oxidoreductase or complex I that is ubiquitously distributed among Cyanobacteria.Semantic proximity Read ↗

Pantoea ananatis carotenoid production confers toxoflavin tolerance and is regulated by Hfq-controlled quorum sensingSemantic proximity Read ↗

Proteomic alterations explain phenotypic changes in Sinorhizobium meliloti lacking the RNA chaperone Hfq.Semantic proximity Read ↗

Only one dnaK homolog, dnaK2, is active transcriptionally and is essential in Synechocystis.Semantic proximity Read ↗

Chlorophyll a phytylation is required for the stability of photosystems I and II in the cyanobacterium Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Biosynthesis of menaquinone (vitamin K2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms.Semantic proximity Read ↗

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