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Literature summary for 5.4.3.8 extracted from

  • Berry-Lowe, S.L.; Grimm, B.; Smith, M.A.; Kannangara, C.G.
    Purification and characterization of glutamate 1-semialdehyde aminotransferase from barley expressed in Escherichia coli (1992), Plant Physiol., 99, 1597-1603.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Hordeum vulgare

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
(S)-4-Amino-5-oxopentanoate
-
Hordeum vulgare

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-4-Amino-5-oxopentanoate Hordeum vulgare 4,5-diaminovalerate may be an intermediate in the synthesis of 5-amino-4-oxopentanoate ?
-
?
(S)-4-Amino-5-oxopentanoate Hordeum vulgare enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate ?
-
?

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Hordeum vulgare

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.384
-
-
Hordeum vulgare

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-4-Amino-5-oxopentanoate
-
Hordeum vulgare 5-Amino-4-oxopentanoate
-
?
(S)-4-Amino-5-oxopentanoate 4,5-diaminovalerate may be an intermediate in the synthesis of 5-amino-4-oxopentanoate Hordeum vulgare ?
-
?
(S)-4-Amino-5-oxopentanoate enzyme catalyzes the last step in the conversion of Glu to 5-amino-4-oxopentanoate Hordeum vulgare ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.11
-
(S)-4-Amino-5-oxopentanoate
-
Hordeum vulgare