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Literature summary for 5.4.3.8 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

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

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-4-Amino-5-oxopentanoate Escherichia coli 4,5-dioxovalerate and 4,5-diaminovalerate are reaction intermediates ?
-
?

Organism

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli