Spectroscopic method for measuring activity of cis-aconitate decarboxylase, an important metabolic regulator of immune responses.

Kevin Knowlan, Cody L Hoop, Nadya I Tarasova

Abstract read

In one paragraph

Article in Analytical biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Kevin KnowlanCancer Innovation Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, P.O. Box B, Frederick, MD, 21702, USA. Electronic address: kevin.knowlan@nih.gov.

Cody L HoopCancer Innovation Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, P.O. Box B, Frederick, MD, 21702, USA. Electronic address: cody.hoop@nih.gov.

Nadya I TarasovaCancer Innovation Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, P.O. Box B, Frederick, MD, 21702, USA. Electronic address: nadya.tarasova@nih.gov.

Funding

Inhibitors of protein-protein interactionsZIABC011306 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI TARASOVA, NADYA · 2010 to 2025

$7.3M

Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC011306

6 · The paper itself

Abstract

Cis-aconitate decarboxylase (ACOD1) is a key enzyme converting cis-aconitate to itaconate, which has therapeutic potential for inflammatory diseases. Existing methods to measure ACOD1 activity and itaconate are often expensive and complex. We developed a novel, high-throughput spectrophotometric assay using the Fürth-Herrmann reaction. Our method quantifies ACOD1-catalyzed itaconate production by leveraging distinct absorbance ratios of cis-aconitate and itaconate at 386 nm and 440 nm. We optimized parameters, characterized human ACOD1 kinetics, and determined an IC

Indexed as

Carboxy-LyasesEnzyme AssaysAconitic AcidHumansKineticsSpectrophotometry, UltravioletSuccinatesaconitate decarboxylaseAconitic AcidCarboxy-Lyasesitaconic acidSuccinatescis-aconitate decarboxylase (ACOD1)Immune-Responsive Gene 1 (IRG1)ItaconateSpectrophotometry

Identifiers

PMID40653293

DOI10.1016/j.ab.2025.115944

PMCPMC12323396

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.