Literature summary for 4.2.3.119 extracted from

Tashiro, M.; Kiyota, H.; Kawai-Noma, S.; Saito, K.; Ikeuchi, M.; Iijima, Y.; Umeno, D.
Bacterial production of pinene by a laboratory-evolved pinene-synthase (2016), ACS Synth. Biol., 5, 1011-1020 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene PT1, recombinant expression of His-tagged enzyme from codon-optimized gene in Escherichia coli cytosol, coexpression of prenyltransferases GPP synthase and FPP synthase	Pinus taeda

Protein Variants

Protein Variants	Comment	Organism
H346Y	site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), no phenotype, similar to wild-type	Pinus taeda
additional information	estalishment of a pinene production system in recombinant Escherichia coli by coexpression of (-)-alpha-pinene synthase from Pinus paeda and Abies grandis GPPS, as well as farnesyl diphosphate synthase mutant IspA(S80F) from Escherichia coli. The isolated alpha-pinene synthase variant PSmut outperforms the wild-type (parent) enzyme in multiple contexts in Escherichia coli and cyanobacteria. The purified variant exhibits drastically altered metal dependency, enabling to keep the activity in the cytosol that is manganese-deficient. Coexpression of this variant with mevalonate pathway enzymes, isopentenyl diphosphate isomerase, and GPP synthase yield 140 mg/l pinene in a flask culture. Screening for PS mutants with higher cellular activity and production method optimization, overview	Pinus taeda
Q456L	site-directed mutagenesis, mutation in the alpha-domain (catalytic domain), the mutant shows a reduction in pigmentation (PSmut) but shows improved catalytic activity	Pinus taeda

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0014	-	geranyl diphosphate	pH and temperature not specified in the publication	Pinus taeda

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Pinus taeda

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
geranyl diphosphate	Pinus taeda	-	(-)-alpha-pinene + diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pinus taeda	Q84KL6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
geranyl diphosphate	-	Pinus taeda	(-)-alpha-pinene + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
pinene-synthase	-	Pinus taeda
PT1	-	Pinus taeda

General Information

General Information	Comment	Organism
malfunction	mutation Q456L in the alpha-domain (catalytic domain) causes a reduction in pigmentation (PSmut)	Pinus taeda
additional information	Q457 is located on helix F, which supports a part of the catalytic core and is proximate to the highly conserved residues Y455 and E458	Pinus taeda

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Release 2023.1 (January 2023)