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

BRENDA support

Literature summary for 5.4.3.8 extracted from

  • Smith, M.A.; Kannangara, C.G.; Grimm, B.; von Wettstein, D.
    Characterization of glutamate-1-semialdehyde aminotransferase of Synechococcus. Steady-state kinetic analysis (1991), Eur. J. Biochem., 202, 749-757.
    View publication on PubMed
Search for more literature for 5.4.3.8

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
4,5-Dioxovalerate competitive inhibition of pyridoxamine-phosphate form of the enzyme and mixed-type inhibition of the pyridoxal-phosphate form of the enzyme Synechococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
 4,5-Diaminovalerate
-
 Synechococcus sp.
0.067
-
 (S)-4-Amino-5-oxopentanoate
-
 Synechococcus sp.
1.4
-
 4,5-Dioxovalerate
-
 Synechococcus sp.

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-glutamate 1-semialdehyde = 5-aminolevulinate ping-pong bi-bi mechanism in which 4,5-diaminovalerate is the second substrate and 4,5-dioxovalerate is an alternative first substrate Synechococcus sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-4-Amino-5-oxopentanoate
-
 Synechococcus sp. 5-Amino-4-oxopentanoate
-
 ?
4,5-Diaminovalerate is a substrate for the pyridoxal 5'-phosphate form of the enzyme Synechococcus sp. ?
-
 ?
4,5-Dioxovalerate is a substrate for the pyridoxamine form of the enzyme Synechococcus sp. 5-Amino-4-oxopentanoate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.95
-
 (S)-4-Amino-5-oxopentanoate
-
 Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxamine 5'-phosphate the pyridoxal-phosphate form of the enzyme and the pyridoxamine-phosphate form of the enzyme are similarly active Synechococcus sp.