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Information on EC 4.2.3.121 - (+)-alpha-pinene synthase and Organism(s) Lavandula angustifolia and UniProt Accession Q2XSC6

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.121 (+)-alpha-pinene synthase
IUBMB Comments
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-alpha-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-beta-pinene synthase, and EC 4.2.3.116, (+)-camphene synthase.
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This record set is specific for:
Lavandula angustifolia
UNIPROT: Q2XSC6
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Word Map
  • 4.2.3.121
  • adenylyl
  • olfactory
  • odor
  • aciii
  • nucleotide-gated
  • cyclases
  • cilium
  • ciliogenesis
  • ciliopathy
  • vomeronasal
  • golf
  • +-alpha-pinene
The taxonomic range for the selected organisms is: Lavandula angustifolia
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclase iii, (+)-alpha-pinene cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
limonene synthase
-
(+)-alpha-pinene cyclase
-
-
-
-
cyclase I
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-alpha-pinene-forming]
Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-alpha-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-alpha-pinene and (+)-beta-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-alpha-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-beta-pinene synthase, and EC 4.2.3.116, (+)-camphene synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
11637-21-3
-
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 39% (R)-(+)-limonene, 22% terpinolene, 16% (1R,5S)-(+)-camphene, 14% (1R,5R)-(+)-alpha-pinene, 8% beta-myrcene and traces of alpha-phellandrene. Preferential formation of the (+)-enantiomers with 94% enantiomeric purity for (1R,5R)-(+)-alpha-pinene. Product pattern changes to 46% limonene, 9% terpinolene, 23% alpha-pinene, 5% beta-myrcene and 4% alpha-phellandrene, when Mn2+ is supplied instead of Mg2+
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
or Mn2+, required, optimum concentration 50 mM
Mn2+
or Mg2+, required, optimum concentration 0.2 mM. 68% of the efficiency with Mg2+, with change in product pattern to 46% limonene, 9% terpinolene, 23% alpha-pinene, 5% beta-myrcene and 4% alpha-phellandrene, for Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0474
geranyl diphosphate
pH 7.5, 23°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
geranyl diphosphate
pH 7.5, 23°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.253
geranyl diphosphate
pH 7.5, 23°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
optimum for maximum formation of alpha-pinene
7
optimum for total enzymic activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
optimum for total enzymic activity
33
optimum for maximum formation of alpha-pinene
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LALIM_LAVAN
602
0
70345
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70300
x * 70300, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70300, calculated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Landmann, C.; Fink, B.; Festner, M.; Dregus, M.; Engel, K.H.; Schwab, W.
Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia)
Arch. Biochem. Biophys.
465
417-429
2007
Lavandula angustifolia (Q2XSC6)
Manually annotated by BRENDA team