EC 4.2.3.132 - Neoabietadiene synthase

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IntEnz Enzyme Nomenclature
EC 4.2.3.132

Names

Accepted name:
neoabietadiene synthase
Other names:
AgAS
PtTPS-LAS
Systematic name:
(+)-copaly-diphosphate diphosphate-lyase (cyclizing, neoabietadiene-forming)

Reaction

Comments:

Isolated from Abies grandis (grand fir) [1]. This class I enzyme forms about equal proportions of abietadiene, levopimaradiene and neoabietadiene. See also EC 4.2.3.18, abieta-7,13-diene synthase and EC 4.2.3.32, levopimaradiene synthase. An X-ray study of this multifunctional enzyme showed that the class I activity is in the α domain, while (+)-copalyl diphosphate synthase activity (EC 5.5.1.12, a class II activity) is in the β and γ domains [2]. In Pinus taeda (loblolly pine) the major product is levopimaradiene, with less abietadiene and neoabietadiene [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Peters, R. J., Flory, J. E., Jetter, R., Ravn, M. M., Lee, H. J., Coates, R. M., Croteau, R. B.
    Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the "pseudomature" recombinant enzyme.
    Biochemistry 39 : 15592-15602 (2000). [PMID: 11112547]
  2. Zhou, K., Gao, Y., Hoy, J. A., Mann, F. M., Honzatko, R. B., Peters, R. J.
    Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis.
    J. Biol. Chem. 287 : 6840-6850 (2012). [PMID: 22219188]
  3. Ro, D. K., Bohlmann, J.
    Diterpene resin acid biosynthesis in loblolly pine (Pinus taeda): functional characterization of abietadiene/levopimaradiene synthase (PtTPS-LAS) cDNA and subcellular targeting of PtTPS-LAS and abietadienol/abietadienal oxidase (PtAO, CYP720B1).
    Phytochemistry 67 : 1572-1578 (2006). [PMID: 16497345]

[EC 4.2.3.132 created 2012]