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Literature summary for 5.4.3.8 extracted from

  • Rieble, S.; Beale, S.I.
    Separation and partial characterization of enzymes catalyzing delta-aminolevulinic acid formation in Synechocystis sp. PCC 6803 (1991), Arch. Biochem. Biophys., 289, 289-297.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
gabaculine 0.0005 mM, 50% inhibition. The inhibition is reversible up to 1 h after its addition, if the gabaculine is removed by gel filtration, before the enzyme is incubated by gel filtration, before the enzyme is incubated with substrate. Irreversible inhibition is obtained by preincubation of the enzyme at 30°C either for several hours with gabaculine alone or for a few min with both gabaculine and glutamate-1-semialdehyde Synechococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
98000
-
gel filtration Synechococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-4-Amino-5-oxopentanoate Synechococcus sp. one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
PCC 6803
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00009
-
-
Synechococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-4-Amino-5-oxopentanoate
-
Synechococcus sp. 5-Amino-4-oxopentanoate
-
?
(S)-4-Amino-5-oxopentanoate one of three enzymes in formation of 5-aminolevulinic acid from Glu via the five-carbon pathway Synechococcus sp. ?
-
?