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aminoadipate-semialdehyde dehydrogenase

Known as: L Aminoadipate Semialdehyde Dehydrogenase, L-Aminoadipate-Semialdehyde Dehydrogenase, 2-Aminoadipate Reductase 
An enzyme that catalyzes the oxidation of L-2-aminoadipate 6-semialdehyde to L-2-aminoadipate (alpha-aminoadipic acid). It is involved in the… Expand
National Institutes of Health

Papers overview

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Highly Cited
2010
Highly Cited
2010
The microbial degradation of phenol by pure cultures Bacillus cereus MTCC 9817 strain AKG1 and B. cereus MTCC 9818 strain AKG2 is… Expand
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Highly Cited
2006
Highly Cited
2006
We show here that children with pyridoxine-dependent seizures (PDS) have mutations in the ALDH7A1 gene, which encodes antiquitin… Expand
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Review
2003
Review
2003
Summary. Glutamic semialdehyde is a product of oxidation of arginine and proline, and aminoadipic semialdehyde, of oxidation of… Expand
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Highly Cited
1983
Highly Cited
1983
1. The effects of the ionophoretic application of a number of excitatory amino acids and antagonists to the dendrites of CA1… Expand
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Highly Cited
1979
Highly Cited
1979
Normal strains of Saccharomyces cerevisiae do not use alpha-aminoadipate as a principal nitrogen source. However, alpha… Expand
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Highly Cited
1977
Highly Cited
1977
IN retina as in brain, the metabolism of glutamic acid and γ-aminobutyric acid (GABA) is compartmentalised in biochemically… Expand
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Highly Cited
1976
Highly Cited
1976
Abstract Mice susceptible to ‘audiogenic’ seizures (DBA/2, 21–25 days old) were treated with either di-n-propylacetate. DPA, (200… Expand
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Highly Cited
1972
Highly Cited
1972
The genetic basis of the biodegradation of salicylate in Pseudomonas putida R1 has been studied. This strain utilizes the meta… Expand
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Highly Cited
1971
Highly Cited
1971
1 Catechol was metabolized through 2-hydroxymuconic semialdehyde by cell-free extracts of benzoate-grown Azotobacter Strains… Expand
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Highly Cited
1964
Highly Cited
1964
In 1953, succinic semialdehyde was demonstrated to be an intermediate in the metabolism of y-aminobutyric acid by mammalian brain… Expand
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