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Literature summary for 1.1.1.36 extracted from

  • Olavarria, K.; Carnet, A.; van Renselaar, J.; Quakkelaar, C.; Cabrera, R.; Guedes da Silva, L.; Smids, A.L.; Villalobos, P.A.; van Loosdrecht, M.C.M.; Wahl, S.A.
    An NADH preferring acetoacetyl-CoA reductase is engaged in poly-3-hydroxybutyrate accumulation in Escherichia coli (2021), J. Biotechnol., 325, 207-216 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Candidatus Accumulibacter phosphatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0077
-
NADH recombinant enzyme, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.0443
-
NADPH recombinant enzyme, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.0567
-
acetoacetyl-CoA recombinant enzyme, with NADH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.318
-
acetoacetyl-CoA recombinant enzyme, with NADPH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-3-hydroxybutyryl-CoA + NAD+ Candidatus Accumulibacter phosphatis
-
acetoacetyl-CoA + NADH + H+
-
r
(R)-3-hydroxybutyryl-CoA + NAD+ Candidatus Accumulibacter phosphatis UW-1
-
acetoacetyl-CoA + NADH + H+
-
r
acetoacetyl-CoA + NADH + H+ Candidatus Accumulibacter phosphatis
-
(R)-3-hydroxybutyryl-CoA + NAD+
-
r
acetoacetyl-CoA + NADH + H+ Candidatus Accumulibacter phosphatis UW-1
-
(R)-3-hydroxybutyryl-CoA + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Candidatus Accumulibacter phosphatis C7RM91
-
-
Candidatus Accumulibacter phosphatis UW-1 C7RM91
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.07
-
native enzyme, forward reaction, using NADPH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.25
-
recombinant enzyme, forward reaction, using NADPH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.61
-
native enzyme, backward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
1.96
-
recombinant enzyme, forward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
14
-
native enzyme, forward reaction, using NADH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-3-hydroxybutyryl-CoA + NAD+
-
Candidatus Accumulibacter phosphatis acetoacetyl-CoA + NADH + H+
-
r
(R)-3-hydroxybutyryl-CoA + NAD+
-
Candidatus Accumulibacter phosphatis UW-1 acetoacetyl-CoA + NADH + H+
-
r
acetoacetyl-CoA + NADH + H+
-
Candidatus Accumulibacter phosphatis (R)-3-hydroxybutyryl-CoA + NAD+
-
r
acetoacetyl-CoA + NADH + H+
-
Candidatus Accumulibacter phosphatis UW-1 (R)-3-hydroxybutyryl-CoA + NAD+
-
r
acetoacetyl-CoA + NADPH + H+
-
Candidatus Accumulibacter phosphatis (R)-3-hydroxybutyryl-CoA + NADP+
-
?
acetoacetyl-CoA + NADPH + H+
-
Candidatus Accumulibacter phosphatis UW-1 (R)-3-hydroxybutyryl-CoA + NADP+
-
?
additional information no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor Candidatus Accumulibacter phosphatis ?
-
-
additional information no oxidation of (R/S)-3-hydroxybutyryl-CoA is detected when using NADP+ as cofactor Candidatus Accumulibacter phosphatis UW-1 ?
-
-

Synonyms

Synonyms Comment Organism
AAR
-
Candidatus Accumulibacter phosphatis
NADH-preferring acetoacetyl-CoA reductase
-
Candidatus Accumulibacter phosphatis
PhaB
-
Candidatus Accumulibacter phosphatis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.095
-
NADPH recombinant enzyme, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
0.131
-
acetoacetyl-CoA recombinant enzyme, with NADPH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
8.92
-
NADH recombinant enzyme, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis
11.6
-
acetoacetyl-CoA recombinant enzyme, with NADH as cosubstrate, at pH 7.5 and 25°C Candidatus Accumulibacter phosphatis

Cofactor

Cofactor Comment Organism Structure
NADH the enzyme clearly prefers NADH over NADPH Candidatus Accumulibacter phosphatis