Literature summary for 1.3.1.81 extracted from

Ringer, K.L.; McConkey, M.E.; Davis, E.M.; Rushing, G.W.; Croteau, R.
Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint (2003), Arch. Biochem. Biophys., 418, 80-92.

Search for more literature for 1.3.1.81

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3)	Mentha x piperita

General Stability

General Stability	Organism
neither protease inhibitors nor flavins improve the activity or stability of the purified native enzyme, and the addition of glycerol to the buffers leads to rapid loss of activity upon storage	Mentha x piperita

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0023	-	(+)-pulegone	pH 5.0, recombinant enzyme	Mentha x piperita
0.0069	-	NADPH	pH 5.0, recombinant enzyme	Mentha x piperita

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
37914	-	1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation	Mentha x piperita
43000	-	1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation	Mentha x piperita
45000	-	gel filtration	Mentha x piperita

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 (+)-pulegone + 2 NADPH + 2 H+	Mentha x piperita	pathways of monoterpene biosynthesis, overview	(-)-menthone + (+)-isomenthone + 2 NADP+	-	?

Organism

Organism	UniProt	Comment	Textmining
Mentha x piperita	-	cv. Black Mitcham	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21(DE3), native enzyme by oil gland secretory cell isolation procedure, two steps of anion exchange chromatography, hydroxyapatite chromatography, and beta-NADPH affinity chromatography, the activity is rapidly lost during purification on each matrix, 10fold purification accompanied by loss of over 98% of starting activity	Mentha x piperita

Source Tissue

Source Tissue	Comment	Organism	Textmining
epidermis	-	Mentha x piperita	-
leaf	-	Mentha x piperita	-
secretory cell	-	Mentha x piperita	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 (+)-pulegone + 2 NADPH + 2 H+	pathways of monoterpene biosynthesis, overview	Mentha x piperita	(-)-menthone + (+)-isomenthone + 2 NADP+	-	?
2 (+)-pulegone + 2 NADPH + 2 H+	the reductase catalyzes the reduction of the 4(8)-double bond of (+)-pulegone to produce both (-)-menthone and (+)-isomenthone in a 70:30 ratio, product analysis by GC-MS, stereospecific reductase	Mentha x piperita	(-)-menthone + (+)-isomenthone + 2 NADP+	-	?

Subunits

Subunits	Comment	Organism
monomer	1 x * 43000, SDS-PAGE, 1 * 37914, sequence calculation	Mentha x piperita

Synonyms

Synonyms	Comment	Organism
More	(+)-pulegone reductase is a member of the medium-chain dehydrogenase/reductase superfamily	Mentha x piperita
pulegone reductase	-	Mentha x piperita

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.8	-	NADPH	pH 5.0, recombinant enzyme	Mentha x piperita
1.8	-	(+)-pulegone	pH 5.0, recombinant enzyme	Mentha x piperita

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	-	-	Mentha x piperita

pH Range

pH Minimum	pH Maximum	Comment	Organism
4.5	6.5	70% of maximal activity within this range	Mentha x piperita

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	dependent on	Mentha x piperita

pI Value

Organism	Comment	pI Value Maximum	pI Value
Mentha x piperita	about, isoelectric focusing	-	5.2

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Release 2023.1 (January 2023)