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4043-91-8

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4043-91-8 Usage

General Description

D-3-Hydroxykynurenine is an intermediate in the pathway of tryptophan metabolism. It is produced from L-tryptophan by the enzyme tryptophan 2,3-dioxygenase and serves as a precursor to the neuroactive compound kynurenic acid. D-3-Hydroxykynurenine is also involved in the generation of reactive oxygen species, which can lead to oxidative stress and damage to cells. Additionally, it has been implicated in the pathogenesis of various neurodegenerative and psychiatric disorders. Studies have shown that dysregulation of D-3-Hydroxykynurenine metabolism may contribute to the development of conditions such as Alzheimer's disease, Parkinson's disease, and depression. Therefore, understanding the biochemical and physiological roles of D-3-Hydroxykynurenine is crucial for the development of potential therapeutic interventions for these disorders.

Check Digit Verification of cas no

The CAS Registry Mumber 4043-91-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,0,4 and 3 respectively; the second part has 2 digits, 9 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 4043-91:
(6*4)+(5*0)+(4*4)+(3*3)+(2*9)+(1*1)=68
68 % 10 = 8
So 4043-91-8 is a valid CAS Registry Number.

4043-91-8Upstream product

4043-91-8Relevant articles and documents

A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin

Giessen, Tobias W.,Kraas, Femke I.,Marahiel, Mohamed A.

experimental part, p. 5680 - 5692 (2012/05/19)

The antitumor antibiotic sibiromycin belongs to the class of pyrrolo[1,4]benzodiazepines (PBDs) that are produced by a variety of actinomycetes. PBDs are sequence-specific DNA-alkylating agents and possess significant antitumor properties. Among them, sibiromycin, one of two identified glycosylated PBDs, displays the highest DNA binding affinity and the most potent antitumor activity. In this study, we report the elucidation of the precise reaction sequence leading to the formation and activation of the 3,5-dihydroxy-4-methylanthranilic acid building block found in sibiromycin, starting from the known metabolite 3-hydroxykynurenine (3HK). The investigated pathway consists of four enzymes, which were biochemically characterized in vitro. Starting from 3HK, the SAM-dependent methyltransferase SibL converts the substrate to its 4-methyl derivative, followed by hydrolysis through the action of the PLP-dependent kynureninase SibQ, leading to 3-hydroxy-4-methylanthranilic acid (3H4MAA) formation. Subsequently the NRPS didomain SibE activates 3H4MAA and tethers it to its thiolation domain, where it is hydroxylated at the C5 position by the FAD/NADH-dependent hydroxylase SibG yielding the fully substituted anthranilate moiety found in sibiromycin. These insights about sibiromycin biosynthesis and the substrate specificities of the biosynthetic enzymes involved may guide future attempts to engineer the PBD biosynthetic machinery and help in the production of PBD derivatives.

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