Human aldehyde oxidase 1 / AOX1

evidence_span

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experimental_model

Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification

exposure

Retinaldehyde with/without NAD+; selective inhibitors

limitations

Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens

plain_language

Different enzymes share vitamin A processing, and their contributions depend on the conditions.

primary_references

[mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296

tissue_or_cell_type

Purified enzyme and liver S9 fractions

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 911–922

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification · source_derived_draft · unverified_draft

### mo-aox-aldh-partition In human liver S9, AOX inhibition reduced retinoic-acid formation by 20-50%, versus 50-80% with ALDH1A1 inhibition; AOX had lower affinity and higher capacity. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Different enzymes share vitamin A processing, and their contributions depend on the conditions. organism: Homo sapiens tissue_or_cell_type: Purified enzyme and liver S9 fractions experimental_model: Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification limitations: Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage. exposure: Retinaldehyde with/without NAD+; selective inhibitors evidence_span: {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"} [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296

evidence_span

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experimental_model

Human liver cytosolic fractionation, proteomics, inhibitors and docking

exposure

GDC-0834 amide-hydrolysis assays

limitations

AO and carboxylesterase both implicated; docking proposes a mechanism but does not prove every catalytic step.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens

plain_language

AOX1 can participate in drug breakdown beyond simple aldehyde oxidation.

primary_references

[mo-p25845827] A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834. (2015). https://pubmed.ncbi.nlm.nih.gov/25845827/ DOI: 10.1124/dmd.114.061804

tissue_or_cell_type

Liver cytosol

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 924–935

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human liver cytosolic fractionation, proteomics, inhibitors and docking · source_derived_draft · unverified_draft

### mo-aox-amide Inhibitor and fractionation experiments implicated AO and carboxylesterase, but not XOR, in GDC-0834 amide hydrolysis. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 can participate in drug breakdown beyond simple aldehyde oxidation. organism: Homo sapiens tissue_or_cell_type: Liver cytosol experimental_model: Human liver cytosolic fractionation, proteomics, inhibitors and docking limitations: AO and carboxylesterase both implicated; docking proposes a mechanism but does not prove every catalytic step. exposure: GDC-0834 amide-hydrolysis assays evidence_span: {"source_cache": "artifacts/molybdenum-research/25845827.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40", "start_char": 0, "end_char": 1619, "text_sha256": "8f5a9632067829ecae57508a9127fb042a6467165c3fc494fdd44be975dadf40"} [mo-p25845827] A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834. (2015). https://pubmed.ncbi.nlm.nih.gov/25845827/ DOI: 10.1124/dmd.114.061804

evidence_span

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experimental_model

Human AOX1 structures and steady-state kinetics with substrate and inhibitor

exposure

Phthalazine and thioridazine

limitations

Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

AOX1 processes certain nitrogen-containing compounds.

primary_references

[mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895

tissue_or_cell_type

Recombinant purified AOX1

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 833–844

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 structures and steady-state kinetics with substrate and inhibitor · source_derived_draft · unverified_draft

### mo-aox-phthalazine Human AOX1 structures and kinetics characterize phthalazine binding and oxidation at its molybdenum active site. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 processes certain nitrogen-containing compounds. organism: Homo sapiens protein tissue_or_cell_type: Recombinant purified AOX1 experimental_model: Human AOX1 structures and steady-state kinetics with substrate and inhibitor limitations: Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements. exposure: Phthalazine and thioridazine evidence_span: {"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"} [mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895

evidence_span

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experimental_model

Biochemical fractionation of four human livers and three kidneys

exposure

Retinaldehyde and other aldehyde substrate assays

limitations

Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens

plain_language

AOX1 intersects vitamin A chemistry, alongside other enzymes.

primary_references

[mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366

tissue_or_cell_type

Liver and kidney soluble extracts

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 885–896

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical fractionation of four human livers and three kidneys · source_derived_draft · unverified_draft

### mo-aox-retinal A separable aldehyde-oxidase fraction accounted for some NAD-independent retinaldehyde metabolism in human liver and kidney extracts. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: AOX1 intersects vitamin A chemistry, alongside other enzymes. organism: Homo sapiens tissue_or_cell_type: Liver and kidney soluble extracts experimental_model: Biochemical fractionation of four human livers and three kidneys limitations: Biochemical enzyme-fraction identification predates modern isoform assays; does not establish AOX1 as the dominant human retinoic-acid source or mineral-responsive route. exposure: Retinaldehyde and other aldehyde substrate assays evidence_span: {"source_cache": "artifacts/molybdenum-research/10559215.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238", "start_char": 0, "end_char": 1879, "text_sha256": "a0a70e022e9499ca5d0608c1da80afadfad2215ac6cf1219c8ce8da3280a5238"} [mo-p10559215] Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. (1999). https://pubmed.ncbi.nlm.nih.gov/10559215/ DOI: 10.1074/jbc.274.47.33366

evidence_span

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experimental_model

Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification

exposure

Retinaldehyde with/without NAD+; selective inhibitors

limitations

Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens

plain_language

A molybdenum enzyme can contribute to making vitamin A signaling molecules.

primary_references

[mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296

tissue_or_cell_type

Purified enzyme and liver S9 fractions

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 898–909

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification · source_derived_draft · unverified_draft

### mo-aox-retinoic-acid Recombinant human AOX converted all-trans-retinaldehyde to all-trans-retinoic acid, with an apparent Km near 1.5 micromolar. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A molybdenum enzyme can contribute to making vitamin A signaling molecules. organism: Homo sapiens tissue_or_cell_type: Purified enzyme and liver S9 fractions experimental_model: Recombinant human AOX and human liver S9 kinetics, inhibitors and protein quantification limitations: Ex-vivo contribution depends on substrate and NAD+ availability; no dietary molybdenum intervention or universal in-vivo percentage. exposure: Retinaldehyde with/without NAD+; selective inhibitors evidence_span: {"source_cache": "artifacts/molybdenum-research/33355213.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2", "start_char": 0, "end_char": 2211, "text_sha256": "0edb31bff85231dfbde4a99d6858db611c099d2cd00982cad88616aa960b5aa2"} [mo-p33355213] Aldehyde Oxidase Contributes to All-Trans-Retinoic Acid Biosynthesis in Human Liver. (2021). https://pubmed.ncbi.nlm.nih.gov/33355213/ DOI: 10.1124/dmd.120.000296

evidence_span

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experimental_model

Human AOX1 variant crystallography and CD/ThermoFAD stability assays

exposure

Wild type compared with SNP variants

limitations

In-vitro structures and thermal stability; not physiological temperature or diet thresholds.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

The molybdenum enzyme also contains a riboflavin-derived cofactor.

primary_references

[mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617

tissue_or_cell_type

Purified AOX1

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 859–870

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 variant crystallography and CD/ThermoFAD stability assays · source_derived_draft · unverified_draft

### mo-aox-fad AOX1-bound FAD acted as the intrinsic fluorescence reporter in ThermoFAD unfolding assays. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: The molybdenum enzyme also contains a riboflavin-derived cofactor. organism: Homo sapiens protein tissue_or_cell_type: Purified AOX1 experimental_model: Human AOX1 variant crystallography and CD/ThermoFAD stability assays limitations: In-vitro structures and thermal stability; not physiological temperature or diet thresholds. exposure: Wild type compared with SNP variants evidence_span: {"source_cache": "artifacts/molybdenum-research/30985987.fulltext.txt", "locator": "Exact primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d187787b0c042c674903c56275b485ee23c2b3545ed1c0ed02ca0cd2e3abb7c0", "start_char": 11532, "end_char": 12101, "text_sha256": "13ae767e495f8efc3a6c44005156563bc471d8aec37486330086d3fed343ef38"} [mo-p30985987] Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019). https://pubmed.ncbi.nlm.nih.gov/30985987/ DOI: 10.1002/2211-5463.12617

evidence_span

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experimental_model

Human AOX1 structures and steady-state kinetics with substrate and inhibitor

exposure

Phthalazine and thioridazine

limitations

Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens protein

plain_language

A drug can inhibit AOX1 at a site separate from its substrate reaction.

primary_references

[mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895

tissue_or_cell_type

Recombinant purified AOX1

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 846–857

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human AOX1 structures and steady-state kinetics with substrate and inhibitor · source_derived_draft · unverified_draft

### mo-aox-inhibition Thioridazine bound a distinct noncompetitive inhibitor site in human AOX1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A drug can inhibit AOX1 at a site separate from its substrate reaction. organism: Homo sapiens protein tissue_or_cell_type: Recombinant purified AOX1 experimental_model: Human AOX1 structures and steady-state kinetics with substrate and inhibitor limitations: Specific xenobiotic chemistry; does not establish broad detoxification benefits from molybdenum supplements. exposure: Phthalazine and thioridazine evidence_span: {"source_cache": "artifacts/molybdenum-research/26322824.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188", "start_char": 0, "end_char": 1067, "text_sha256": "0c289f1d166c7335431b4d041963accf22af348b4cac506145f2ccef59ca8188"} [mo-p26322824] Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. (2015). https://pubmed.ncbi.nlm.nih.gov/26322824/ DOI: 10.1038/nchembio.1895

evidence_span

{"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"}

experimental_model

Gene identification in two type II xanthinuria patients and comparison subjects

exposure

MOCOS Arg419 stop mutation

limitations

Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis.

nutrient_topic

Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum

organism

Homo sapiens

plain_language

Two molybdenum enzymes need an additional sulfur-activation step.

primary_references

[mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719

tissue_or_cell_type

Liver cDNA and patient genetics

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 521–532

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Gene identification in two type II xanthinuria patients and comparison subjects · source_derived_draft · unverified_draft

### mo-mocos-sulfuration MOCOS defects in type II xanthinuria support its role in supplying the terminal sulfur required by XDH and AOX1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Two molybdenum enzymes need an additional sulfur-activation step. organism: Homo sapiens tissue_or_cell_type: Liver cDNA and patient genetics experimental_model: Gene identification in two type II xanthinuria patients and comparison subjects limitations: Genetic evidence for terminal sulfuration; type II xanthinuria is different from loss of all Moco synthesis. exposure: MOCOS Arg419 stop mutation evidence_span: {"source_cache": "artifacts/molybdenum-research/11302742.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3", "start_char": 0, "end_char": 1011, "text_sha256": "8f595c96d16b055cd6b9611c4d036626222ffb084ec778f840255cac57ecdfb3"} [mo-p11302742] Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. (2001). https://pubmed.ncbi.nlm.nih.gov/11302742/ DOI: 10.1006/bbrc.2001.4719