ArticleThe Journal of biological chemistry2019
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- The Kynurenine Pathway: Unraveling Its Role in Neurological Disorders via Mammalian Cellular Models.International journal of molecular sciences · 2026Review
- α-Amino-β-carboxymuconate-ε-semialdehyde decarboxylase catalyzes enol/keto tautomerization of oxaloacetate.The Journal of biological chemistry · 2024Article
- Adaptable SEC-SAXS data collection for higher quality structure analysis in solution.Protein science : a publication of the Protein Society · 2024Article
- Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes.Current opinion in chemical biology · 2023Review
- Kynurenine Pathway Regulation at Its Critical Junctions with Fluctuation of Tryptophan.Metabolites · 2023Article
- Controlling Enzymatic Activity by Modulating the Oligomerization State via Chemical Rescue and Optical Control.Chembiochem : a European journal of chemical biology · 2022Article
- Structural Basis of Human Dimeric α-Amino-β-Carboxymuconate-ε-Semialdehyde Decarboxylase Inhibition With TES-1025.Frontiers in molecular biosciences · 2022Article
- Diflunisal Derivatives as Modulators of ACMS Decarboxylase Targeting the Tryptophan-Kynurenine Pathway.Journal of medicinal chemistry · 2021Article
- Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
α-Amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) plays an important role in l-tryptophan degradation via the kynurenine pathway. ACMSD forms a homodimer and is functionally inactive as a monomer because its catalytic assembly requires an arginine residue from a neighboring subunit. However, how the oligomeric state and self-association of ACMSD are controlled in solution remains unexplored. Here, we demonstrate that ACMSD from
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Registered trials
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.