Arylformamidase

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Arylformamidase
Identifiers
EC number3.5.1.9
CAS number9025-05-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum


Arylformamidase is an enzyme that catalyzes the hydrolysis of arylformamides to produce formic acid and an arylamine. This enzyme is part of the hydrolase family, specifically those acting on carbon-nitrogen bonds, other than peptide bonds, in linear amides. It plays a crucial role in the tryptophan catabolism pathway, which is essential for the metabolism of this important amino acid.

Function[edit | edit source]

Arylformamidase is involved in the kynurenine pathway, which is the primary route of tryptophan degradation in mammals. This pathway leads to the production of nicotinamide adenine dinucleotide (NAD+), a vital coenzyme in cellular metabolism. The enzyme specifically catalyzes the conversion of N-formylkynurenine to kynurenine by removing the formyl group as formic acid.

Structure[edit | edit source]

The structure of arylformamidase has been studied in various organisms, revealing that it typically consists of a single polypeptide chain. The active site of the enzyme contains residues that are crucial for binding the substrate and facilitating the hydrolysis reaction. Structural studies, often using X-ray crystallography, have provided insights into the enzyme's mechanism of action.

Clinical Significance[edit | edit source]

Dysregulation of the kynurenine pathway, in which arylformamidase is involved, has been associated with several diseases, including neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, as well as psychiatric disorders like depression and schizophrenia. Understanding the role of arylformamidase in these conditions could lead to new therapeutic targets.

Research[edit | edit source]

Ongoing research is focused on understanding the detailed mechanism of arylformamidase and its role in human health and disease. Studies are also exploring the potential of modulating this enzyme's activity as a therapeutic strategy for diseases associated with tryptophan metabolism.

Also see[edit | edit source]



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Contributors: Prab R. Tumpati, MD