Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Smith, M.A.; King, P.J.; Grimm, B.
    Transient-state kinetic analysis of Synechococcus glutamate 1-semialdehyde aminotransferase (1998), Biochemistry, 37, 319-329.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.8 expression in Escherichia coli Synechococcus sp.

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 Synechococcus sp. involved in conversion of glutamate to 5-aminolevulinate 5-aminolevulinate
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.8 Synechococcus sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.3.8 recombinant GSAT Synechococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.8 (S)-4-amino-5-oxopentanoate
-
Synechococcus sp. 5-aminolevulinate
-
r
5.4.3.8 (S)-4-amino-5-oxopentanoate involved in conversion of glutamate to 5-aminolevulinate Synechococcus sp. 5-aminolevulinate
-
r

Synonyms

EC Number Synonyms Comment Organism
5.4.3.8 GSAT
-
Synechococcus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.8 pyridoxal 5'-phosphate
-
Synechococcus sp.