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

Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase.

Biochemistry - 24 Jun 2003

Louie Tai Man, Xie X Sunney, Xun Luying

Abstract excerpt

4-Hydroxyphenylacetate (4HPA) 3-monooxygenase (HpaB) is a reduced flavin adenine dinucleotide (FADH(2)) utilizing monooxygenase. Its cosubstrate, FADH(2), is supplied by HpaC, an NAD(P)H-flavin oxidoreductase. Because HpaB is the first enzyme for 4HPA metabolism, FADH(2) production and utilizatio...

Read the complete abstract on PubMed

Topics

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

Share to Flavin-Adenine Dinucleotide
Share to FMN Reductase
Share to Mixed Function Oxygenases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Phenylacetates

Share to Plasmids

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 12809507
DOI: 10.1021/bi034092r

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12809507-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase.PMID 12809507Read ↗

Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme, p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumanniiSemantic proximity Read ↗

Formate hydrogenlyase is needed for proton-potassium exchange through the F0F1-ATPase and the TrkA system in anaerobically grown and glycolysing Escherichia coli.Semantic proximity Read ↗

The Inhibitory Effect of Cyclodextrin on Oxygen Bioavailability Is a Key Factor for the Metabolic Flux Redistribution Toward Steroid Alcohols in Phytosterol Resting Cells Bioconversion.Semantic proximity Read ↗

Dynamic interactive events in gene regulation using E. coli dehydrogenase as a model.Semantic proximity Read ↗

New FadB homologous enzymes and their use in enhanced biosynthesis of medium-chain-length polyhydroxyalkanoates in FadB mutant Escherichia coli.Semantic proximity Read ↗

Transcriptional control of hydrogen production during mixed carbon fermentation by hydrogenases 4 (hyf) and 3 (hyc) in Escherichia coli.Semantic proximity Read ↗

Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase.Semantic proximity Read ↗

A two-component hydroxylase involved in the assimilation of 3-hydroxyphenyl acetate in Pseudomonas putida.Semantic proximity Read ↗

Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli.Semantic proximity Read ↗

Relationship between formate hydrogen lyase and proton-potassium pump under heterolactic fermentation in Escherichia coli: functional multienzyme associations in the cell membrane.Semantic proximity Read ↗

In silico prediction and validation of the importance of the Entner-Doudoroff pathway in poly(3-hydroxybutyrate) production by metabolically engineered Escherichia coli.Semantic proximity Read ↗

Involvement of mitochondrial ferredoxin and para-aminobenzoic acid in yeast coenzyme Q biosynthesis.Semantic proximity Read ↗

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