Component
Acinetobacter baumannii CntA carnitine monooxygenase component
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
Acinetobacter baumannii CntA/CntB catalyzed oxygen-dependent carnitine cleavage to TMA and malic semialdehyde.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified bacterial enzyme complex, spectroscopy and mutagenesis.
- limitations
- This aerobic chemistry is not assumed to dominate the anoxic colon.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- A separate microbial route needs oxygen.
- primary_references
- Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 386–392
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bacterial enzyme complex, spectroscopy and mutagenesis. · source_derived_draft · unverified_draft
## l-carnitine-cnta-cleavage A separate microbial route needs oxygen. Acinetobacter baumannii CntA/CntB catalyzed oxygen-dependent carnitine cleavage to TMA and malic semialdehyde. Model: Purified bacterial enzyme complex, spectroscopy and mutagenesis. Limitations: This aerobic chemistry is not assumed to dominate the anoxic colon. Evidence access: Primary abstract Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266
Complete structured claim and evidence
What acts on it
CntB passed NADH-derived electrons through FMN and iron-sulfur centers to support CntA oxygen activation.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Acinetobacter enzyme redox spectroscopy and site-directed mutants.
- limitations
- Bacterial cofactor dependence does not show that human B2 or iron supplementation increases TMAO.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- Riboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry.
- primary_references
- Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 394–400
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Acinetobacter enzyme redox spectroscopy and site-directed mutants. · source_derived_draft · unverified_draft
## l-carnitine-cntb-redox Riboflavin-derived FMN, iron centers and NADH connect to microbial carnitine chemistry. CntB passed NADH-derived electrons through FMN and iron-sulfur centers to support CntA oxygen activation. Model: Acinetobacter enzyme redox spectroscopy and site-directed mutants. Limitations: Bacterial cofactor dependence does not show that human B2 or iron supplementation increases TMAO. Evidence access: Primary abstract Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32694223/ · DOI 10.1074/jbc.RA120.014266
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.