KEGG   ENZYME: 4.2.3.125Help
Entry
EC 4.2.3.125                Enzyme                                 

Name
alpha-muurolene synthase;
Cop3
Class
Lyases;
Carbon-oxygen lyases;
Acting on phosphates
BRITE hierarchy
Sysname
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, alpha-muurolene-forming)
Reaction(IUBMB)
(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate [RN:R10004]
Reaction(KEGG)
Substrate
(2E,6E)-farnesyl diphosphate [CPD:C00448]
Product
alpha-muurolene [CPD:C20272];
diphosphate [CPD:C00013]
Comment
The enzyme has been characterized from the fungus Coprinus cinereus. Also gives germacrene A and gamma-muurolene, see EC 4.2.3.23, germacrene-A synthase and EC 4.2.3.126, gamma-muurolene synthase.
History
EC 4.2.3.125 created 2012
Orthology
K21927  alpha-muurolene/germacrene-A/gamma-muurolene synthase
Genes
TVS: TRAVEDRAFT_75578
DSQ: DICSQDRAFT_124305
SHS: STEHIDRAFT_45387
HIR: HETIRDRAFT_167573
FME: FOMMEDRAFT_109318
GTR: GLOTRDRAFT_103889
MPR: MPER_06109
MRR: Moror_15644 Moror_7733
CCI: CC1G_12294
ABP: AGABI1DRAFT46681(AGABI1DRAFT_46681)
ABV: AGABI2DRAFT73543(AGABI2DRAFT_73543)
 » show all
Taxonomy
Reference
1  [PMID:19400802]
  Authors
Agger S, Lopez-Gallego F, Schmidt-Dannert C
  Title
Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus.
  Journal
Mol Microbiol 72:1181-95 (2009)
DOI:10.1111/j.1365-2958.2009.06717.x
  Sequence
Reference
2  [PMID:20889795]
  Authors
Lopez-Gallego F, Wawrzyn GT, Schmidt-Dannert C
  Title
Selectivity of fungal sesquiterpene synthases: role of the active site's H-1 alpha loop in catalysis.
  Journal
Appl Environ Microbiol 76:7723-33 (2010)
DOI:10.1128/AEM.01811-10
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.2.3.125
IUBMB Enzyme Nomenclature: 4.2.3.125
ExPASy - ENZYME nomenclature database: 4.2.3.125
BRENDA, the Enzyme Database: 4.2.3.125

DBGET integrated database retrieval system