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

Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes.

Cell biochemistry and biophysics - 1 Jan 2013

Serrano Ana, Frago Susana, Herguedas Beatriz, Martínez-Júlvez Marta, Velázquez-Campoy Adrián, Medina Milagros

Abstract excerpt

Many known prokaryotic organisms depend on a single bifunctional enzyme, encoded by the RibC of RibF gene and named FAD synthetase (FADS), to convert Riboflavin (RF), first into FMN and then into FAD. The reaction occurs through the sequential action of two activities present on a single polypept...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Catalytic Domain
Share to Corynebacterium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Flavin Mononucleotide

Share to Mutagenesis, Site-Directed

Share to Nucleotidyltransferases

Share to Phosphotransferases (Alcohol Group Acceptor)

Source

Identifiers

PMID: 22892871
DOI: 10.1007/s12013-012-9403-9

Genes

RFK

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22892871-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes.PMID 22892871Read ↗

Role of key residues at the flavin mononucleotide (FMN):adenylyltransferase catalytic site of the bifunctional riboflavin kinase/flavin adenine dinucleotide (FAD) Synthetase from Corynebacterium ammoniagenes.Semantic proximity Read ↗

Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.Semantic proximity Read ↗

Complex structure of Bacillus subtilis RibG: the reduction mechanism during riboflavin biosynthesis.Semantic proximity Read ↗

The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon.Semantic proximity Read ↗

Archaeal RibL: a new FAD synthetase that is air sensitive.Semantic proximity Read ↗

Structural characterization of ribT from Bacillus subtilis reveals it as a GCN5-related N-acetyltransferase.Semantic proximity Read ↗

Identification of riboflavin: revealing different metabolic characteristics between Escherichia coli BL21(DE3) and MG1655.Semantic proximity Read ↗

[Mutational analysis of the ribC gene of Bacillus subtilis].Semantic proximity Read ↗

Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC.Semantic proximity Read ↗

A single change in the aptamer of the Lactiplantibacillus plantarum rib operon riboswitch severely impairs its regulatory activity and leads to a vitamin B2 - overproducing phenotype.Semantic proximity Read ↗

Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain.Semantic proximity Read ↗

[Multifunctional regulatory mutation in Bacillus subtilis flavinogenesis system].Semantic proximity Read ↗

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