L-aminoadipate-semialdehyde dehydrogenase

L-aminoadipate-semialdehyde dehydrogenase
Alpha-aminoadipic semialdehyde dehydrogenase tetramer, Human
Identifiers
EC no.1.2.1.31
CAS no.9067-87-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
H2O
H+
 
 

The three substrates of this enzyme are L-2-aminoadipate 6-semialdehyde (L-allysine), oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are (S)-α-aminoadipic acid, reduced NADH, and a proton. This enzyme can also use nicotinamide adenine dinucleotide phosphate as its cofactor.[1][2]

The enzyme participates in lysine biosynthesis and biodegradation.[3]

Nomenclature

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase. Other names in common use include:

  • aminoadipate semialdehyde dehydrogenase,
  • 2-aminoadipate semialdehyde dehydrogenase,
  • alpha-aminoadipate-semialdehyde dehydrogenase,
  • alpha-aminoadipate reductase,
  • 2-aminoadipic semialdehyde dehydrogenase,
  • L-alpha-aminoadipate delta-semialdehyde oxidoreductase,
  • L-alpha-aminoadipate delta-semialdehyde:NAD+ oxidoreductase,
  • L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine,
  • and dinucleotide oxidoreductase.

References

  1. ^ Enzyme 1.2.1.31 at KEGG Pathway Database.
  2. ^ Calvert AF, Rodwell VW (1966). "Metabolism of pipecolic acid in a Pseudomonas species. 3 L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase". J. Biol. Chem. 241 (2): 409–14. doi:10.1016/S0021-9258(18)96932-2. PMID 4285660.
  3. ^ Voet, Donald; Voet, Judith G. (2011). Biochemistry (4th ed.). Hoboken, NJ: Wiley. pp. 1040–41. ISBN 978-0-470-91745-9.