Literature summary for 1.1.1.1 extracted from

Suwannarangsee, S.; Kim, S.; Kim, O.C.; Oh, D.B.; Seo, J.W.; Kim, C.H.; Rhee, S.K.; Kang, H.A.; Chulalaksananukul, W.; Kwon, O.
Characterization of alcohol dehydrogenase 3 of the thermotolerant methylotrophic yeast Hansenula polymorpha (2012), Appl. Microbiol. Biotechnol., 96, 697-709.

Cloned(Commentary)

Cloned (Comment)	Organism
gene ADH3, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His6-tagged enzyme in Echerichia coli strain BL21 (DE3), complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, semi-quantitative RT-PCR analysis	Ogataea angusta

Cloned (Comment)

Organism

gene ADH3, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His6-tagged enzyme in Echerichia coli strain BL21 (DE3), complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, semi-quantitative RT-PCR analysis

Ogataea angusta

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of the ADH3 deletion mutant, complementation of the HpADH3 mutant by an HpADH3 expression cassette fused to a strong constitutive promoter, the resulting strain produced a significantly increased amount of ethanol compared to the wild-type strain in a glucose medium, while in a xylose medium, the ethanol production is dramatically reduced in an HpADH3 overproduction strain compared to that in the wild-type strain, phenotype analysis of DELTAHpADH3 and DELTAHpADH1/DELTAHpADH3 mutants, overview	Ogataea angusta

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.45	-	ethanol	pH 9.0, 22°C, recombinant enzyme	Ogataea angusta
0.67	-	acetaldehyde	pH 6.0, 22°C, recombinant enzyme	Ogataea angusta

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	HpADH3	Ogataea angusta	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
acetaldehyde + NADH + H+	Ogataea angusta	-	ethanol + NAD+	-	r
acetaldehyde + NADH + H+	Ogataea angusta DL-1	-	ethanol + NAD+	-	r
ethanol + NAD+	Ogataea angusta	-	acetaldehyde + NADH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Ogataea angusta	H9ZGN0	i.e. Pichia angusta, HpADH3 is not the major ADH in strain DL-1, gene ADH3	-
Ogataea angusta DL-1	H9ZGN0	i.e. Pichia angusta, HpADH3 is not the major ADH in strain DL-1, gene ADH3	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Echerichia coli strain BL21 (DE3) by nickel affinity chromatography	Ogataea angusta

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
1,2-butanediol + NAD+	low activity	Ogataea angusta	?	-	?
1,2-butanediol + NAD+	low activity	Ogataea angusta DL-1	?	-	?
1-butanol + NAD+	-	Ogataea angusta	butanal + NADH + H+	-	r
1-butanol + NAD+	-	Ogataea angusta DL-1	butanal + NADH + H+	-	r
1-octanol + NAD+	-	Ogataea angusta	octanal + NADH + H+	-	r
1-pentanol + NAD+	-	Ogataea angusta	pentanal + NADH + H+	-	r
1-propanol + NAD+	-	Ogataea angusta	propanaldehyde + NADH + H+	-	r
2-methoxyethanol + NAD+	-	Ogataea angusta	2-methoxyacetaldehyde + NADH + H+	-	r
2-octanol + NAD+	low activity	Ogataea angusta	2-octanone + NADH + H+	-	r
2-pentanol + NAD+	low activity	Ogataea angusta	2-pentanone + NADH + H+	-	r
2-propanol + NAD+	-	Ogataea angusta	2-propanone + NADH + H+	-	r
acetaldehyde + NADH + H+	-	Ogataea angusta	ethanol + NAD+	-	r
acetaldehyde + NADH + H+	best substrate	Ogataea angusta	ethanol + NAD+	-	r
acetaldehyde + NADH + H+	-	Ogataea angusta DL-1	ethanol + NAD+	-	r
acetaldehyde + NADH + H+	best substrate	Ogataea angusta DL-1	ethanol + NAD+	-	r
ethanol + NAD+	-	Ogataea angusta	acetaldehyde + NADH + H+	-	r
additional information	methanol, formaldehyde, and acetone are no substrates for HpADH3	Ogataea angusta	?	-	?
additional information	methanol, formaldehyde, and acetone are no substrates for HpADH3	Ogataea angusta DL-1	?	-	?

Synonyms

Synonyms	Comment	Organism
alcohol dehydrogenase 3	-	Ogataea angusta
HpADH3	-	Ogataea angusta

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Ogataea angusta

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
3000	-	ethanol	pH 9.0, 22°C, recombinant enzyme	Ogataea angusta
3500	-	acetaldehyde	pH 6.0, 22°C, recombinant enzyme	Ogataea angusta

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	aldehyde reduction	Ogataea angusta
9	-	alcohol oxidation	Ogataea angusta

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Ogataea angusta
NADH	-	Ogataea angusta

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
6667	-	ethanol	pH 9.0, 22°C, recombinant enzyme	Ogataea angusta
70000	-	acetaldehyde	pH 6.0, 22°C, recombinant enzyme	Ogataea angusta