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Literature summary extracted from

  • Tyacke, R.J.; Harwood, J.L.; John, R.A.
    Properties of the pyridoxaldimine form of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1-aminomutase) and analysis of its role as an intermediate in the formation of aminolaevulinate (1993), Biochem. J., 293, 697-791.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.3.8 (S)-4-Amino-5-oxopentanoate Pisum sativum enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.8 Pisum sativum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.3.8 L-glutamate 1-semialdehyde = 5-aminolevulinate mechanism Pisum sativum
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.8 (S)-4-Amino-5-oxopentanoate
-
 Pisum sativum 5-Amino-4-oxopentanoate
-
 ?
5.4.3.8 (S)-4-Amino-5-oxopentanoate enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate Pisum sativum ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.8 pyridoxamine 5'-phosphate conversion into the active pyridoxamine-phosphate form of enzyme in an exponential process Pisum sativum