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Literature summary extracted from

  • Hempel, J.; Kraut, A.; Wymore, T.
    Gamma glutamyl semialdehyde dehydrogenase: Simulations on native and mutant forms support the importance of outer shell lysines (2009), Chem. Biol. Interact., 178, 75-78.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.2.1.41 medicine in humans a natural S352L mutation gives rise to type II hyperprolinemia, mental retardation Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NAD+ Thermus thermophilus
-
L-glutamyl 5-phosphate + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.41 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.41 L-glutamate 5-semialdehyde + phosphate + NAD+
-
Thermus thermophilus L-glutamyl 5-phosphate + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.41 hexamer composed by dimers Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.2.1.41 ALDH4
-
Thermus thermophilus
1.2.1.41 gamma glutamyl semialdehyde dehydrogenase
-
Thermus thermophilus
1.2.1.41 GGSALDH
-
Thermus thermophilus
1.2.1.41 pyrroline 5-carboxylate dehydrogenase
-
Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.41 NAD+ the work based on a computer simulation using a PDB data set of Thermus thermophilus GGSALDH, pdb2BJA, in this structure the enzyme is co-crystallized with NADH Thermus thermophilus