Literature summary for 1.2.1.42 extracted from

Lan, E.; Ro, S.; Liao, J.
Oxygen-tolerant coenzyme A-acylating aldehyde dehydrogenase facilitates efficient photosynthetic n-butanol biosynthesis in cyanobacteria (2013), Energy Environ. Sci., 6, 2672-2681 .

No PubMed abstract available

Cloned(Commentary)

Cloned (Comment)	Organism
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 does not result in autotrophic n-butanol production, the enzyme from Porphyromonas gingivalis cannot enable anaerobic growth rescue	Porphyromonas gingivalis

Cloned (Comment)

Organism

gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 does not result in autotrophic n-butanol production, the enzyme from Porphyromonas gingivalis cannot enable anaerobic growth rescue

Porphyromonas gingivalis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.076	-	acetyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis
0.256	-	butanoyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + NADH + H+	Porphyromonas gingivalis	-	acetaldehyde + CoA + NAD+	-	r
butanoyl-CoA + NADH + H+	Porphyromonas gingivalis	-	butanal + CoA + NAD+	-	r

Organism

Organism	UniProt	Comment	Textmining
Porphyromonas gingivalis	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the enzyme is oxygen-tolerant	Porphyromonas gingivalis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.2	-	about, with butanoyl-CoA, pH 7.15, 30°C	Porphyromonas gingivalis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetyl-CoA + NADH + H+	-	Porphyromonas gingivalis	acetaldehyde + CoA + NAD+	-	r
butanoyl-CoA + NADH + H+	-	Porphyromonas gingivalis	butanal + CoA + NAD+	-	r
additional information	substrate chain length specificity of the enzyme is C2-C12, highest activity with C12 substrate, overview. The overall activity of the enzyme is low compared to other PduP enzymes	Porphyromonas gingivalis	?	-	?

Synonyms

Synonyms	Comment	Organism
CoA-acylating aldehyde dehydrogenase	-	Porphyromonas gingivalis
coenzyme A-acylating aldehyde dehydrogenase	-	Porphyromonas gingivalis
PduP	-	Porphyromonas gingivalis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Porphyromonas gingivalis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.08	-	acetyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis
0.19	-	butanoyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.15	-	assay at	Porphyromonas gingivalis

Cofactor

Cofactor	Comment	Organism	Structure
NADH	-	Porphyromonas gingivalis

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.7	-	butanoyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis
1.1	-	acetyl-CoA	recombinant enzyme, pH 7.15, 30°C	Porphyromonas gingivalis