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Information on EC 4.2.3.119 - (-)-alpha-pinene synthase and Organism(s) Picea sitchensis and UniProt Accession Q6XDB5

for references in articles please use BRENDA:EC4.2.3.119
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.119 (-)-alpha-pinene synthase
IUBMB Comments
Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-alpha-pinene and (-)-beta-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-alpha-pinene and 20% (-)-beta-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-alpha-pinene with traces of (-)-beta-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-alpha-pinene and 30% (-)-beta-pinene . The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-alpha-pinene and (-)-camphene plus traces of other monoterpenoids . See also EC 4.2.3.120, (-)-beta-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-beta-phellandrene synthase.
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This record set is specific for:
Picea sitchensis
UNIPROT: Q6XDB5
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The taxonomic range for the selected organisms is: Picea sitchensis
The enzyme appears in selected viruses and cellular organisms
Synonyms
mono-tps, plpin, avtps1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(-)-alpha-pinene cyclase
-
-
-
-
(-)-alpha-pinene/(-)-camphene synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-alpha-pinene-forming]
Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-alpha-pinene and (-)-beta-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-alpha-pinene and 20% (-)-beta-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-alpha-pinene with traces of (-)-beta-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-alpha-pinene and 30% (-)-beta-pinene [13]. The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-alpha-pinene and (-)-camphene plus traces of other monoterpenoids [14]. See also EC 4.2.3.120, (-)-beta-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-beta-phellandrene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
110637-20-2
for both EC 4.2.3.119 and 4.2.3.120
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
geranyl diphosphate
(-)-alpha-pinene + diphosphate
show the reaction diagram
-
products are (-)-alpha-pinene and (-)-beta-pinene, in a ratio of about 35:10
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PINS2_PICSI
627
0
71384
Swiss-Prot
Chloroplast (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
significant increase in transcript level in the leaders of lateral branches of weevil-attacked and mechanically wounded trees
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McKay, S.A.; Hunter, W.L.; Godard, K.A.; Wang, S.X.; Martin, D.M.; Bohlmann, J.; Plant, A.L.
Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce
Plant Physiol.
133
368-378
2003
Picea sitchensis (Q6XDB5), Picea sitchensis
Manually annotated by BRENDA team