L-aminoadipate-semialdehyde dehydrogenase

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L-aminoadipate-semialdehyde dehydrogenase
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Alpha-aminoadipic semialdehyde dehydrogenase tetramer, Human
Identifiers
EC no. 1.2.1.31
CAS no. 9067-87-2
Databases
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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Gene Ontology AmiGO / QuickGO
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In enzymology, a L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
L-aminoadipate-semialdehyde dehydrogenase
H2O
H+
 
+ NADH
 

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:

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.