Aminocarboxymuconate-semialdehyde decarboxylase

The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction

aminocarboxymuconate-semialdehyde decarboxylase
aminocarboxymuconate-semialdehyde decarboxylase dimer, Human
Identifiers
EC no.4.1.1.45
CAS no.37289-47-7
Alt. namesACMSD
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate 2-aminomuconate semialdehyde + CO2

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in tryptophan metabolism. It has been identified as a marker in nonverbal autism.[1]

Nomenclature edit

The systematic name of this enzyme class is 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming). Other names in common use include picolinic acid carboxylase, picolinic acid decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehade decarboxylase, alpha-amino-beta-carboxymuconate-epsilon-semialdehyde, beta-decarboxylase, 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase, and 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase.

References edit

  1. ^ Kainer, David; Templeton, Alan R.; Prates, Erica T.; Jacboson, Daniel; Allan, Euan R.O.; Climer, Sharlee; Garvin, Michael R. (2023). "Structural variants identified using non-Mendelian inheritance patterns advance the mechanistic understanding of autism spectrum disorder". Human Genetics and Genomics Advances. 4 (1): 100150. doi:10.1016/j.xhgg.2022.100150. PMC 9634371. PMID 36340933.

Further reading edit