Target type: biologicalprocess
Any process that modulates the frequency, rate or extent of 'de novo' NAD biosynthetic process from tryptophan. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:12140278, PMID:19843166]
The de novo biosynthesis of NAD+ from tryptophan is a complex process involving multiple enzymatic steps and is essential for maintaining cellular redox homeostasis and energy metabolism. This pathway begins with the conversion of tryptophan to kynurenine by the enzyme tryptophan 2,3-dioxygenase (TDO) or indoleamine 2,3-dioxygenase (IDO). Kynurenine is then sequentially metabolized to quinolinate by a series of enzymatic reactions, including kynurenine 3-monooxygenase (KMO), kynureninase (KYNU), and 3-hydroxyanthranilate 3,4-dioxygenase (HAAO). Quinolinate is then converted to nicotinate mononucleotide (NaMN) by the enzyme quinolinate phosphoribosyltransferase (QPRT). NaMN is subsequently converted to nicotinamide adenine dinucleotide (NAD+) by a series of enzymatic reactions, including NaMN adenylyltransferase (NMNAT) and NAD synthase (NADSYN).
The regulation of this pathway is complex and involves a variety of mechanisms, including transcriptional regulation, post-translational modification, and allosteric regulation. For example, the expression of TDO and IDO can be induced by inflammatory cytokines, such as interferon-gamma (IFN-γ), and by the presence of tryptophan in the environment. The activity of KMO can be inhibited by nicotinamide, the precursor of NAD+, and by other metabolites, such as quinolinate. The activity of KYNU can be inhibited by the presence of kynurenine, while the activity of HAAO can be inhibited by the presence of 3-hydroxyanthranilate.
In addition to these regulatory mechanisms, the de novo biosynthesis of NAD+ from tryptophan can be influenced by other factors, such as the availability of substrate, the presence of cofactors, and the pH of the environment.
Overall, the regulation of the de novo biosynthesis of NAD+ from tryptophan is a complex process that involves multiple enzymatic steps and is subject to a variety of regulatory mechanisms. This pathway is essential for maintaining cellular redox homeostasis and energy metabolism and is therefore critical for cell survival and function.'
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Protein | Definition | Taxonomy |
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2-amino-3-carboxymuconate-6-semialdehyde decarboxylase | A 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8TDX5] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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diflunisal | diflunisal : An organofluorine compound comprising salicylic acid having a 2,4-difluorophenyl group at the 5-position. Diflunisal: A salicylate derivative and anti-inflammatory analgesic with actions and side effects similar to those of ASPIRIN. | monohydroxybenzoic acid; organofluorine compound | non-narcotic analgesic; non-steroidal anti-inflammatory drug |
dipicolinic acid | dipicolinic acid : A pyridinedicarboxylic acid carrying two carboxy groups at positions 2 and 6. | pyridinedicarboxylic acid | bacterial metabolite |