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Information on EC 4.2.3.212 - (+)-delta-cadinol synthase
for references in articles please use BRENDA:EC4.2.3.212
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EC Tree 4 Lyases
4.2 Carbon-oxygen lyases
4.2.3 Acting on phosphates
4.2.3.212 (+)-delta-cadinol synthase
IUBMB Comments
The enzyme is involved in the biosynthesis of sesquiterpenoids from (2E,6E)-farnesyl diphosphate in fungi such as Boreostereum vibrans and Coniophora puteana.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
(+)-delta-cadinol synthase, Agr3, Copu5, Copu9, Cun0716, Cun7050, DCS, delta-cadinol synthase, STS3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(+)-delta-cadinol synthase
Copu5
Copu9
DCS
delta-cadinol synthase
delta-cadinol synthase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + H2O = (+)-delta-cadinol + diphosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-delta-cadinol-forming]
The enzyme is involved in the biosynthesis of sesquiterpenoids from (2E,6E)-farnesyl diphosphate in fungi such as Boreostereum vibrans and Coniophora puteana.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
-
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Clitopilus pseudopinsitus
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Kutzneria kofuensis DSM 43851
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
-
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Clitopilus pseudopinsitus
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Substrates: -
Products: -
Products: -
?
(2E,6E)-farnesyl diphosphate + H2O
(+)-delta-cadinol + diphosphate
Kutzneria kofuensis DSM 43851
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00314
(2E,6E)-farnesyl diphosphate
mutant C76V of isoform Copu9, at pH 7.5 and 25°C
0.00442
(2E,6E)-farnesyl diphosphate
mutant N228A of isoform Copu9, at pH 7.5 and 25°C
0.00459
(2E,6E)-farnesyl diphosphate
wild type isoform Copu9, at pH 7.5 and 25°C
0.0051
(2E,6E)-farnesyl diphosphate
mutant S314N of isoform Copu9, at pH 7.5 and 25°C
0.00628
(2E,6E)-farnesyl diphosphate
mutant T73C of isoform Copu9, at pH 7.5 and 25°C
0.00682
(2E,6E)-farnesyl diphosphate
mutant P197C of isoform Copu9, at pH 7.5 and 25°C
0.007
(2E,6E)-farnesyl diphosphate
mutant G194A of isoform Copu9, at pH 7.5 and 25°C
0.00828
(2E,6E)-farnesyl diphosphate
mutant T192N of isoform Copu9, at pH 7.5 and 25°C
0.00848
(2E,6E)-farnesyl diphosphate
mutant C195V of isoform Copu9, at pH 7.5 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0192
(2E,6E)-farnesyl diphosphate
mutant S314N of isoform Copu9, at pH 7.5 and 25°C
0.0262
(2E,6E)-farnesyl diphosphate
mutant N228A of isoform Copu9, at pH 7.5 and 25°C
0.0291
(2E,6E)-farnesyl diphosphate
mutant C76V of isoform Copu9, at pH 7.5 and 25°C
0.0324
(2E,6E)-farnesyl diphosphate
wild type isoform Copu9, at pH 7.5 and 25°C
0.036
(2E,6E)-farnesyl diphosphate
mutant G194A of isoform Copu9, at pH 7.5 and 25°C
0.0381
(2E,6E)-farnesyl diphosphate
mutant P197C of isoform Copu9, at pH 7.5 and 25°C
0.0396
(2E,6E)-farnesyl diphosphate
mutant T192N of isoform Copu9, at pH 7.5 and 25°C
0.0398
(2E,6E)-farnesyl diphosphate
mutant C195V of isoform Copu9, at pH 7.5 and 25°C
0.0502
(2E,6E)-farnesyl diphosphate
mutant T73C of isoform Copu9, at pH 7.5 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.755
(2E,6E)-farnesyl diphosphate
mutant S314N of isoform Copu9, at pH 7.5 and 25°C
4.692
(2E,6E)-farnesyl diphosphate
mutant C195V of isoform Copu9, at pH 7.5 and 25°C
4.782
(2E,6E)-farnesyl diphosphate
mutant T192N of isoform Copu9, at pH 7.5 and 25°C
5.135
(2E,6E)-farnesyl diphosphate
mutant G194A of isoform Copu9, at pH 7.5 and 25°C
5.584
(2E,6E)-farnesyl diphosphate
mutant P197C of isoform Copu9, at pH 7.5 and 25°C
5.94
(2E,6E)-farnesyl diphosphate
mutant N228A of isoform Copu9, at pH 7.5 and 25°C
7.067
(2E,6E)-farnesyl diphosphate
wild type isoform Copu9, at pH 7.5 and 25°C
7.995
(2E,6E)-farnesyl diphosphate
mutant T73C of isoform Copu9, at pH 7.5 and 25°C
9.252
(2E,6E)-farnesyl diphosphate
mutant C76V of isoform Copu9, at pH 7.5 and 25°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the biosynthesis of boreovibrins
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A3G1HQN7_9AGAM
393
0
44058
TrEMBL
other Location (Reliability: 3)
A0A5M3MX24_CONPW
Coniophora puteana (strain RWD-64-598)
341
0
38631
TrEMBL
-
A0A5M3MXY8_CONPW
Coniophora puteana (strain RWD-64-598)
349
0
39427
TrEMBL
-
AGR3_CYCAE
358
0
40819
Swiss-Prot
Secretory Pathway (Reliability: 1)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform Copu9, hanging drop vapor diffusion method, using 15% (w/v) polyethylene glycol 3350, 100 mM Tris/HCl at pH 8.5 and 100 mM Mg formate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C187V
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
C195V
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
C69V
the mutation does not affect the product spectrum of the enzyme
C76V
the mutant of isoform Copu9 shows increased catalytic efficiency compare to the wild type enzyme
G194A
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
N220A
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
N228A
the mutant of isoform Copu9 with reduced catalytic efficiency compared to the wild type enzyme shows the formation of an additional side product, germacrene D-4-ol
P189C
the variant of isoform Copu5 exhibits lower product formation compared to the wild type enzyme
P197C
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
S306N
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
S314N
the mutant of isoform Copu9 with reduced catalytic efficiency compared to the wild type enzyme shows the formation of an additional side product, germacrene D-4-ol
T184N
the mutation does not affect the product spectrum of the enzyme
T192N
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
T66C
the mutation does not affect the product spectrum of the enzyme
T73C
the mutant of isoform Copu9 shows increased catalytic efficiency compare to the wild type enzyme
C187V
-
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
-
C195V
-
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
-
C69V
-
the mutation does not affect the product spectrum of the enzyme
-
C76V
-
the mutant of isoform Copu9 shows increased catalytic efficiency compare to the wild type enzyme
-
G194A
-
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
-
N220A
-
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
-
S306N
-
the mutant of isoform Copu5 shows the formation of an additional side product, germacrene D-4-ol
-
T192N
-
the mutant of isoform Copu9 shows decreased catalytic efficiency compare to the wild type enzyme
-
T66C
-
the mutation does not affect the product spectrum of the enzyme
-
T73C
-
the mutant of isoform Copu9 shows increased catalytic efficiency compare to the wild type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA bead chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chhalodia, A.K.; Xu, H.; Tabekoueng, G.B.; Gu, B.; Taizoumbe, K.A.; Lauterbach, L.; Dickschat, J.S.
Functional characterisation of twelve terpene synthases from actinobacteria
Beilstein J. Org. Chem.
19
1386-1398
2023
Kutzneria kofuensis (A0A7W9NKN2), Kutzneria kofuensis DSM 43851 (A0A7W9NKN2)
brenda
Wang, S.; Chen, R.; Yuan, L.; Zhang, C.; Liang, D.; Qiao, J.
Molecular and functional analyses of characterized sesquiterpene synthases in mushroom-forming fungi
J. Fungi (Basel)
9
1017
2023
Boreostereum vibrans (A0A3G1HQN7), Cerrena unicolor, Clitopilus pseudopinsitus (A0A4P2VG85), Coniophora puteana (A0A5M3MXY8), Coniophora puteana (A0A5M3MX24), Coniophora puteana RWD-64-598 (A0A5M3MXY8), Coniophora puteana RWD-64-598 (A0A5M3MX24), Cyclocybe aegerita (A0A5Q0QU70)
brenda
Ringel, M.; Dimos, N.; Himpich, S.; Haack, M.; Huber, C.; Eisenreich, W.; Schenk, G.; Loll, B.; Brueck, T.
Biotechnological potential and initial characterization of two novel sesquiterpene synthases from Basidiomycota Coniophora puteana for heterologous production of delta-cadinol
Microb. Cell Fact.
21
64
2022
Coniophora puteana (A0A5M3MXY8), Coniophora puteana (A0A5M3MX24), Coniophora puteana RWD-64-598 (A0A5M3MXY8), Coniophora puteana RWD-64-598 (A0A5M3MX24)
brenda
Zhou, H.; Yang, Y.L.; Zeng, J.; Zhang, L.; Ding, Z.H.; Zeng, Y.
Identification and characterization of a delta-cadinol synthase potentially involved in the formation of boreovibrins in Boreostereum vibrans of Basidiomycota
Nat. Prod. Bioprospect.
6
167-171
2016
Boreostereum vibrans (A0A3G1HQN7)
brenda
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