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Literature summary for 4.1.3.39 extracted from

  • Baker, P.; Carere, J.; Seah, S.Y.
    Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI (2012), Biochemistry, 51, 4558-4567.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
BphJ the aldehyde dehydrogenase BphJ coordinates the catalytic activity of BphI through allostery rather than through aldehyde channeling Paraburkholderia xenovorans

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Paraburkholderia xenovorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.089
-
(S)-4-hydroxy-2-oxopentanoate in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans
0.158
-
(S)-4-hydroxy-2-oxopentanoate in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans

Organism

Organism UniProt Comment Textmining
Paraburkholderia xenovorans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-4-hydroxy-2-oxopentanoate
-
Paraburkholderia xenovorans ethanal + pyruvate
-
?
additional information BphJ forms a heterotetrameric complex with BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel Paraburkholderia xenovorans ?
-
?

Synonyms

Synonyms Comment Organism
BphI
-
Paraburkholderia xenovorans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.79
-
(S)-4-hydroxy-2-oxopentanoate in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans
4.07
-
(S)-4-hydroxy-2-oxopentanoate in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans

Cofactor

Cofactor Comment Organism Structure
NADH BphI is activated in the presence of the BphJ cofactor, NADH, by about 5fold Paraburkholderia xenovorans