Literature summary for 5.4.3.8 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.

Search for more literature for 5.4.3.8

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	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.	involved in conversion of glutamate to 5-aminolevulinate	5-aminolevulinate	-	r

Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GSAT	Synechococcus sp.

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
GSAT	-	Synechococcus sp.

Cofactor

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

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Release 2023.1 (January 2023)