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Literature summary extracted from

  • Ilag, L.L.; Jahn, D.
    Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R (1992), Biochemistry, 31, 7143-7151.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.3.8 ethanolamine stimulates activity of mutant enzyme Lys265Arg Escherichia coli
5.4.3.8 methylamine stimulates activity of mutant enzyme Lys265Arg Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.8 mutant enzyme Lys265Arg, overexpression Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
5.4.3.8 L265E mutant Lys265Arg has 2% of the enzymatic activity compared to the wild-type enzyme, the dimeric structure is not influenced, activity is stimulated by addition of exogenous amines such as ethanolamine and methylamine Escherichia coli

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 Escherichia coli 4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.8 Escherichia coli
-
wild-type and active site mutant K265R
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.8 (S)-4-Amino-5-oxopentanoate
-
Escherichia coli 5-Amino-4-oxopentanoate
-
?
5.4.3.8 (S)-4-Amino-5-oxopentanoate 4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates Escherichia coli ?
-
?
5.4.3.8 4,5-Diaminovalerate is a substrate for the pyridoxal 5'-phosphate form of the enzyme Escherichia coli ?
-
?
5.4.3.8 4,5-Dioxovalerate is a substrate for the pyridoxamine form of the enzyme Escherichia coli 5-Amino-4-oxopentanoate
-
?

Subunits

EC Number Subunits Comment Organism
5.4.3.8 dimer
-
Escherichia coli