Information on EC 4.2.3.125 - alpha-muurolene synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.3.125
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RECOMMENDED NAME
GeneOntology No.
alpha-muurolene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl diphosphate-diphosphate-lyase (cyclizing, alpha-muurolene-forming)
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cop3
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
alpha-muurolene + diphosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
alpha-muurolene + diphosphate
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
additional information
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the enzyme contains the metal-binding DDXXD motif
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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steady-state kinetics, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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flesh and rind, expression analysis in several different genotypes, high level of alpha-muurolene formation in lines Eshkolit Ha'Amaqim and Arava, sesquiterpene compound profiles, detailed overview
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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structural homology modeling of Cop3 using the crystal structure of aristolochene synthase from Aspergillus terreus. Several polar side chains in the H-alpha1 loops of Cop4 and Cop3 move closer to side chains in the metal-binding DDXXD motif
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant Cop3 in Escherichia coli strain JM109
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gene cop3, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain JM109 leading to production of alpha-muurolene
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H255P
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site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows highly altered product profile compared to the wild-type enzyme, it does no longer produce alpha-muurolene but large amounts of germacrene A (77%), overview
K251I
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site-directed mutagenesis, modification of the H-alpha1 loop, the mutant shows only slightly altered product profile compared to the wild-type enzyme, it produces also beta-copaene, cf. EC 4.2.3.127, overview