Target type: biologicalprocess
The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid. [GOC:ai]
The quinolinate biosynthetic process is a crucial metabolic pathway that produces quinolinate, a key precursor for the biosynthesis of NAD+, a vital coenzyme involved in numerous cellular processes. The pathway starts with the condensation of L-aspartate and dihydroxyacetone phosphate (DHAP) catalyzed by the enzyme aspartate 1-decarboxylase (ADC). This reaction generates N-carbamoyl-L-aspartate, which is then converted to N-carbamoyl-β-alanine by the enzyme carbamoylphosphate synthetase II (CPSII). N-carbamoyl-β-alanine is then transformed into quinolinate through a series of enzymatic steps, involving the enzymes quinolinate synthase (QNS) and nicotinamide phosphoribosyltransferase (NAMPT). In humans, the quinolinate biosynthetic pathway is mainly localized in the liver, where it serves as the primary source of NAD+ for the body. However, the pathway also occurs in other tissues like the brain, where it is involved in the synthesis of NAD+ for neuronal function. The quinolinate biosynthetic process is tightly regulated by a complex network of enzymes, metabolites, and signaling pathways to maintain appropriate NAD+ levels, which are essential for maintaining cellular homeostasis and normal physiological function. Dysregulation of this pathway has been implicated in various pathological conditions including cancer, neurodegenerative diseases, and cardiovascular disorders. Research into the molecular mechanisms underlying the quinolinate biosynthetic process has provided insights into the regulation of NAD+ levels and its importance in human health and disease.'
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Protein | Definition | Taxonomy |
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Kynureninase | A kynureninase that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q16719] | Homo sapiens (human) |
3-hydroxyanthranilate 3,4-dioxygenase | A 3-hydroxyanthranilate 3,4-dioxygenase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P46952] | Homo sapiens (human) |
Kynurenine 3-monooxygenase | A kynurenine 3-monooxygenase that is encoded in the genome of human. [PRO:DNx, UniProtKB:O15229] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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3-hydroxykynurenine | 3-hydroxykynurenine : A hydroxykynurenine that is kynurenine substituted by a hydroxy group at position 3. 3-hydroxykynurenine: RN given refers to cpd without isomeric designation hydroxykynurenine : A hydroxy-amino acid that is kynurenine substituted by a single hydroxy group at unspecified position. A "closed" class. | hydroxykynurenine | human metabolite |
2,4-pyridinedicarboxylic acid | lutidinic acid : A pyridinedicarboxylic acid carrying carboxy groups at positions 2 and 4. | pyridinedicarboxylic acid | |
(3-nitrobenzoyl)alanine | (3-nitrobenzoyl)alanine: inhibits kynurenine hydroxylase; structure in first source | ||
tecadenoson | tecadenoson: an A1 adenosine receptor agonist | ||
kynurenine | L-kynurenine : A kynurenine that has L configuration. | amino acid zwitterion; kynurenine; non-proteinogenic L-alpha-amino acid | human metabolite; mouse metabolite; Saccharomyces cerevisiae metabolite |
3-hydroxyhippuric acid | 3-hydroxyhippuric acid: a kynureninase inhibitor; structure in first source m-hydroxyhippuric acid : An N-acylglycine that is hippuric acid (N-benzoylglycine) substituted at position 3 on the phenyl ring by a hydroxy group. | N-acylglycine; phenols | metabolite |
oxalylglycine | N-oxalylglycine : An amino dicarboxylic acid that is iminodiacetic acid with an oxo substituent. It is used as an inhibitor of alpha-ketoglutarate dependent (EC 1.14.11.*) enzymes. oxalylglycine: structure given in first source | amino dicarboxylic acid; N-acylglycine | EC 1.14.11.* (oxidoreductase acting on paired donors, 2-oxoglutarate as one donor, incorporating 1 atom each of oxygen into both donors) inhibitor |
ro 61-8048 | C-nitro compound | ||
Dihydro-beta-erythroidine hydrobromide | indoles |