Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.3.120 - (-)-beta-pinene synthase and Organism(s) Abies grandis and UniProt Accession Q9M7D0

for references in articles please use BRENDA:EC4.2.3.120
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.120 (-)-beta-pinene synthase
IUBMB Comments
Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. The enzyme, which requires Mg2+ (preferred to Mn2+), can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate) [1-4]. The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-alpha-pinene and (-)-beta-pinene [6-9]. Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-beta-pinene, 26% 3-carene, and traces of alpha-pinene . Synthase III from Pinus taeda (loblolly pine) forms (-)-beta-pinene with traces of alpha-pinene and requires Mn2+ and K+ (Mg2+ is ineffective) . A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-beta-pinene with traces of (-)-alpha-pinene . The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-beta-pinene and 70% (-)-alpha-pinene . See also EC 4.2.3.119, (-)-alpha-pinene synthase, EC 4.2.3.117, (-)-camphene synthase, and EC 4.2.3.107 (+)-3-carene synthase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Abies grandis
UNIPROT: Q9M7D0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Abies grandis
The enzyme appears in selected viruses and cellular organisms
Synonyms
(-)-(1S,5S)-pinene synthase, (-)-pinene synthase, ag9, AvPS, AvTPS1, beta-geraniolene synthase, cyclase II, EC 4.1.99.8, EC 4.2.3.14, mono-tps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(-)-(1S,5S)-pinene synthase
-
-
-
-
(-)-pinene synthase
-
beta-geraniolene synthase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-beta-pinene-forming]
Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-alpha-pinene, (-)-beta-pinene and (-)-camphene, plus traces of other monoterpenoids. The enzyme, which requires Mg2+ (preferred to Mn2+), can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate) [1-4]. The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-alpha-pinene and (-)-beta-pinene [6-9]. Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-beta-pinene, 26% 3-carene, and traces of alpha-pinene [10]. Synthase III from Pinus taeda (loblolly pine) forms (-)-beta-pinene with traces of alpha-pinene and requires Mn2+ and K+ (Mg2+ is ineffective) [11]. A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-beta-pinene with traces of (-)-alpha-pinene [5]. The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-beta-pinene and 70% (-)-alpha-pinene [12]. See also EC 4.2.3.119, (-)-alpha-pinene synthase, EC 4.2.3.117, (-)-camphene synthase, and EC 4.2.3.107 (+)-3-carene 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
(-)-beta-pinene + diphosphate
show the reaction diagram
-
42% terpinolene, 18% (-)-alpha-pinene, 11% (-)-limonene, 10% (-)-beta-pinene plus several minor products
-
?
geranyl diphosphate
(-)-beta-pinene + diphosphate
show the reaction diagram
additional information
?
-
entire product set is derived in stereochemically consistent fashion via (-)-3S-linalyl diphosphate as intermediate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
very poor substitute for Mn2+
Mn2+
-
absolutely required, Km value 0.03 mM
additional information
-
Cu2+, Cd2+, Co2+, Ni2+ and Zn2+ are ineffective
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxymercuribenzoate
-
-
alpha-pinene
-
-
diethyldicarbonate
-
-
diphosphate
-
-
phosphate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
geranyl diphosphate
-
pH 7.8, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019
4-hydroxymercuribenzoate
Abies grandis
-
pH 7.8, temperature not specified in the publication
0.64
diethyldicarbonate
Abies grandis
-
pH 7.8, temperature not specified in the publication
0.17
diphosphate
Abies grandis
-
pH 7.8, temperature not specified in the publication
51
phosphate
Abies grandis
-
pH 7.8, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
80% of maximum activity
8.3
-
80% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TPSD9_ABIGR
630
0
72508
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
63000
-
gel filtration
71500
x * 71500, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 62000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a putative plastid targeting signal
proteolytic modification
sequence contains a putative N-terminal plastid targeting signal
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of amino acid sequence onto the crystal structures of tobacco 5-epi-aristolochene synthase and bornyl diphosphate synthase and comparison with (-)-camphene synthase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C372S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C372S/C480S
replacement with corresponding residue of (-)-camphene synthase, 72% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C372S/F597W/S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 99% of wild-type activity. Mutant produces about 80%(-)-alpha-pinene and 10% (-)-beta-pinene
C372S/S485C
replacement with corresponding residue of (-)-camphene synthase, 92% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S
replacement with corresponding residue of (-)-camphene synthase, 97% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
C480S/F597W
replacement with corresponding residue of (-)-camphene synthase, 7% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
C480S/S485C
replacement with corresponding residue of (-)-camphene synthase, 70% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
F597W
replacement with corresponding residue of (-)-camphene synthase, 73% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C
replacement with corresponding residue of (-)-camphene synthase, 100% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene, while the levels of total pinenes remains relatively constant
S485C/F597W
replacement with corresponding residue of (-)-camphene synthase, 68% of wild-type activity. Mutant produces an increased proportion of (-)-alpha-pinene and a correspondingly decreased proportion of (-)-beta-pinene
additional information
replacement of selected amino acid residues in (-)-pinene synthase with the corresponding residues from (-)-camphene synthase in an effort to identify the amino acids responsible for the catalytic diVerences. The approach produces an enzyme in which more than half of the product is channeled through an alternative pathway. Several (-)-pinene synthase to (-)-camphene synthase amino acid substitutions are necessary before catalysis is significantly altered
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, stable at 4°C, in 50 mM Hepes, pH 7.8, for at least 3 weeks, at -20°C, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation after SDS-PAGE in 1% Tween 20
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bohlmann, J.; Steele C.L.; Croteau, R.
Monoterpene synthases from grand fir (Abies grandis): cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase
J. Biol. Chem.
272
21784-21792
1997
Abies grandis (O24475), Abies grandis
Manually annotated by BRENDA team
Gijzen, M.; Lewinsohn, E.; Croteau, R
Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis)
Arch. Biochem. Biophys.
289
267-273
1991
Abies grandis
Manually annotated by BRENDA team
Lewinsohn, E.; Gijzen, M.; Croteau, R.
Wound-inducible pinene cyclase from grand fir: Purification, characterization, and renaturation after SDS-PAGE
Arch. Biochem. Biophys.
293
167-173
1992
Abies grandis
Manually annotated by BRENDA team
Hyat, D.C.; Croteau, R.
Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis
Arch. Biochem. Biophys.
439
222-233
2005
Abies grandis (O24475)
Manually annotated by BRENDA team
Bohlmann, J.; Phillips, M.; Ramachandiran, V.; Katoh, S.; Croteau, R.
cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis)
Arch. Biochem. Biophys.
368
232-243
1999
Abies grandis (Q9M7D0)
Manually annotated by BRENDA team