Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism

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Reassignment of the human aldehyde dehydrogenase ALDH8A1 (ALDH12) to the kynurenine pathway in tryptophan catabolism

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http://www.wikidata.org/entity/Q56592808

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article publié dans la revue scientifique Journal of Biological Chemistry

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im Juni 2018 veröffentlichter wissenschaftlicher Artikel

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scientific article published in Journal of Biological Chemistry

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wetenschappelijk artikel

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наукова стаття, опублікована в червні 2018

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Reassignment of the human alde ...... thway in tryptophan catabolism

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Reassignment of the human aldehyde dehydrogenase ALDH8A1

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Reassignment of the human alde ...... thway in tryptophan catabolism

@en

Reassignment of the human aldehyde dehydrogenase ALDH8A1

@nl

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Reassignment of the human alde ...... thway in tryptophan catabolism

@en

Reassignment of the human aldehyde dehydrogenase ALDH8A1

@nl

P1476

Reassignment of the human alde ...... thway in tryptophan catabolism

@en

P2860

cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog, ALDH12

Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis"

Targeting amino acid metabolism in cancer growth and anti-tumor immune response

Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans

Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence

Evidence for a Dual Role of an Active Site Histidine in α-Amino-β-carboxymuconate-ε-semialdehyde Decarboxylase

Structural Basis for a Cofactor-dependent Oxidation Protection and Catalysis of Cyanobacterial Succinic Semialdehyde Dehydrogenase

The Power of Two: ARGININE 51 AND ARGININE 239* FROM A NEIGHBORING SUBUNIT ARE ESSENTIAL FOR CATALYSIS IN -AMINO- -CARBOXYMUCONATE- -SEMIALDEHYDE DECARBOXYLASE

ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins

Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling

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9594-9603

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scholarly article

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10.1074/JBC.RA118.003320

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English

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P478

293

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P577

2018-06-22T00:00:00Z

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29703752

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P921

cell biology

molecular biology

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6016481

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