KEGG ENZYME: 5.5.1.12

ENZYME: 5.5.1.12

Entry

EC 5.5.1.12                 Enzyme

Name

copalyl diphosphate synthase;
(+)-copalyl-diphosphate lyase (decyclizing)

Class

Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)

Sysname

(+)-copalyl-diphosphate lyase (ring-opening)

Reaction(IUBMB)

geranylgeranyl diphosphate = (+)-copalyl diphosphate [RN:R06298]

Reaction(KEGG)

R06298

Substrate

geranylgeranyl diphosphate [CPD:C00353]

Product

(+)-copalyl diphosphate [CPD:C11901]

Comment

In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase.

History

EC 5.5.1.12 created 2002, modified 2012

Pathway

ec00904

Diterpenoid biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K12927

abietadiene/neoabietadiene/copalyl diphosphate synthase

K14041

levopimaradiene/copalyl diphosphate synthase

K14042

isopimara-7,15-diene synthase /copalyl diphosphate synthase

K18113

miltiradiene synthase / copalyl diphosphate synthase

K19571

levopimaradiene/neoabietadiene/copalyl diphosphate synthase

K20514

phyllocladan-16alpha-ol/copalyl diphosphate synthase

Genes

SMO:	SELMODRAFT_450918

Reference

1 [PMID:11552804]

Authors

Peters RJ1, Ravn MM, Coates RM, Croteau RB

Title

Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites.

Journal

J Am Chem Soc 123:8974-8 (2001)
DOI:10.1021/ja010670k

Sequence

[ag:AAB05407]

Reference

2 [PMID:22027823]

Authors

Sugai Y, Ueno Y, Hayashi K, Oogami S, Toyomasu T, Matsumoto S, Natsume M, Nozaki H, Kawaide H

Title

Enzymatic (13)C labeling and multidimensional NMR analysis of miltiradiene synthesized by bifunctional diterpene cyclase in Selaginella moellendorffii.

Journal

J Biol Chem 286:42840-7 (2011)
DOI:10.1074/jbc.M111.302703

Sequence

[smo:SELMODRAFT_450918]

Reference

3 [PMID:11805316]

Authors

Peters RJ, Croteau RB.

Title

Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement.

Journal

Proc Natl Acad Sci U S A 99:580-4 (2002)
DOI:10.1073/pnas.022627099

Sequence

[ag:AAB05407]

Reference

4 [PMID:12059223]

Authors

Ravn MM, Peters RJ, Coates RM, Croteau R.

Title

Mechanism of abietadiene synthase catalysis: stereochemistry and stabilization of the cryptic pimarenyl carbocation intermediates.

Journal

J Am Chem Soc 124:6998-7006 (2002)
DOI:10.1021/ja017734b

Reference

5 [PMID:11827528]

Authors

Peters RJ, Croteau RB.

Title

Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate.

Journal

Biochemistry 41:1836-42 (2002)
DOI:10.1021/bi011879d

Sequence

[ag:AAB05407]

Other DBs

ExplorEnz - The Enzyme Database:

5.5.1.12

IUBMB Enzyme Nomenclature:

5.5.1.12

ExPASy - ENZYME nomenclature database:

5.5.1.12

BRENDA, the Enzyme Database:

5.5.1.12

CAS:	157972-08-2

DBGET integrated database retrieval system