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Information on EC 4.2.3.121 - (+)-alpha-pinene synthase and Organism(s) Pinus taeda and UniProt Accession Q84KL3

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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:
Pinus taeda
UNIPROT: Q84KL3
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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: Pinus taeda
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclase iii, (+)-alpha-pinene cyclase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(+)-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 97% (+)-alpha-pinene, 3% (-)-alpha-pinene
-
?
geranyl diphosphate
(+)-alpha-pinene + diphosphate
show the reaction diagram
-
-
main product
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
required for optimum activity, NH4+ may substitute
Mg2+
or Mn2+, required. 67% of reaction velocity with Mn2+
Mn2+
or Mg2+, required. Mn2+ is preferred
NH4+
may substitute for K+ for optimum activity
K+
-
required, Km value 7.5 mM
Mn2+
-
absolutely required
additional information
-
not effective: Li+, Na+, Rb+, Cs+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
geranyl diphosphate
-
substrate inhibition above 0.05 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047
geranyl diphosphate
pH 6.5, 31°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
half-maximal reaction velocity
7.5
half-maximal reaction velocity
5.7
-
half-maximal activity
7.9
-
half-maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PT30_PINTA
628
0
71496
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64500
x * 64500, SDS-PAGE of recombinant protein lacking transit peptide
65000
-
gel fitration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 64500, SDS-PAGE of recombinant protein lacking transit peptide
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a putative transit peptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure against the tobacco sesquiterpene synthase 5-epi-aristolochene synthase and the monoterpene synthase bornyl diphosphate synthase from common sage
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Phillips, M.; Savage, T.; Croteau, R.
Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers
Arch. Biochem. Biophys.
372
197-204
1999
Pinus taeda
Manually annotated by BRENDA team
Phillips, M.A.; Wildung, M.R.; Williams, D.C.; Hyatt, D.C.; Croteau, R.
cDNA isolation, functional expression, and characterization of (+)-alpha-pinene synthase and (-)-alpha-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis
Arch. Biochem. Biophys.
411
267-276
2003
Pinus taeda (Q84KL3), Pinus taeda
Manually annotated by BRENDA team