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Literature summary for 1.2.1.31 extracted from

  • Korasick, D.A.; White, T.A.; Chakravarthy, S.; Tanner, J.J.
    NAD+ promotes assembly of the active tetramer of aldehyde dehydrogenase 7A1 (2018), FEBS Lett., 592, 3229-3238 .
    View publication on PubMedView publication on EuropePMC
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium. For reference, the dimer Mr is 111 kDa. Wild-type ALDH7A1 in the absence of any substrates is subjected to SEC-MALS-SAXS analysis using three nominal loading concentrations in the range of 2-8 mg/ml (18-72 microM by dimer Mr). Results of the MALS experiment show the average in-solution Mr increases from 134 kDa to 158 kDa with increasing protein load concentration, consistent with a concentration-dependent dimer-tetramer equilibrium Homo sapiens
110000
-
 dimeric enzyme, gel filtration and mass spectrometry Homo sapiens
184000
-
 tetrameric enzyme, gel filtration and mass spectrometry Homo sapiens
222000
-
 tetrameric enzyme, about, sequence calculation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O Homo sapiens
-
 L-2-aminoadipate + NAD(P)H + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P49419
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-aminoadipate semialdehyde + NAD(P)+ + H2O
-
 Homo sapiens L-2-aminoadipate + NAD(P)H + H+
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 54000, quantitative sedimentation analysis Homo sapiens
More ALDH7A1 forms a dimer-of-dimers tetramer both in crystallo and in solution. NAD+-binding promotes assembly of the ALDH7A1 tetramer and enhances ALDH7A1 tetramerization at micromolar enzyme concentrations. The apoenzyme is mainly dimeric. NAD+-bound ALDH7A1 is predominantly tetrameric. The tetramer is the active form of the enzyme. The catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability. The major peaks correspond to Mr of 110 kDa and 184 kDa, which are both below the theoretical Mr of the tetramer (222 kDa), consistent with an intermediate exchange regime in which free dimer exists in solution simultaneously with a dimer-tetramer equilibrium. The minor species at 2.7S (54 kDa) likely represents a monomer (theoretical Mr of 56 kDa) Homo sapiens
tetramer 4 * 54000, quantitative sedimentation analysis Homo sapiens

Synonyms

Synonyms Comment Organism
aldehyde dehydrogenase 7A1
-
 Homo sapiens
Aldh7a1
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+ NAD+-binding promotes assembly of the ALDH7A1 tetramer Homo sapiens

General Information

General Information Comment Organism
malfunction mutations in the ALDH7A1 gene can cause the autosomal recessive metabolic disease pyridoxine-dependent epilepsy (PDE), which is characterized by seizure activity within days of birth. Although PDE symptoms can be mitigated with high doses of pyridoxine (vitamin B6) and a lysine-restricted diet, many patients have long-lasting and untreatable cognitive disability. The molecular basis of PDE is thought to be due to a buildup of DELTA1-piperideine-6-carboxylate, the cyclic form of the aldehyde substrate of ALDH7A1 Homo sapiens
metabolism human aldehyde dehydrogenase 7A1 (ALDH7A1) catalyzes the final step in lysine catabolism, the NAD+-dependent oxidation of alpha-aminoadipate semialdehyde to alpha-aminoadipate Homo sapiens
physiological function the catalytically active oligomer of ALDH7A1 is assembled on demand in response to cofactor availability Homo sapiens