Information on EC 4.2.3.101 - 7-epi-sesquithujene synthase

for references in articles please use BRENDA:EC4.2.3.101
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The expected taxonomic range for this enzyme is: Zea mays

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EC NUMBER
COMMENTARY hide
4.2.3.101
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RECOMMENDED NAME
GeneOntology No.
7-epi-sesquithujene synthase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = 7-epi-sesquithujene + diphosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase (7-epi-sesquithujene-forming)
The enzyme from Zea mays, variety B73, gives mainly 7-epi-sesquithujene with (S)-beta-bisabolene and traces of other sesquiterpenoids, cf. EC 4.2.3.55 (S)-beta-bisabolene synthase. It requires Mg2+ or Mn2+. The product ratio is dependent on which metal ion is present. 7-epi-Sesquithujene is an attractant for the emerald ash borer beetle.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
inbred line B73
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
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LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
7-epi-sesquithujene + diphosphate
show the reaction diagram
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7-epi-sesquithujene is the main product, the enzyme also produces (S)-beta-bisabolene, (E)-beta-farnesene, and the minor products sesquithujene, (Z)-alpha-bergamotene, sesquisabinene B, (E)-alpha-bergamotene, and sesquisabinene A
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?
geranyl diphosphate
(S)-(-)-limonene + diphosphate
show the reaction diagram
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main product is (S)-(-)-limonene, minor products are alpha-thujene, beta-myrcene, (+)-sabinene, (-)-sabinene, alpha-terpinene, (E)-beta-ocimene, beta-phellandrene, alpha-terpinolene, gamma-terpinene, sabinene hydrate, (R)-(-)-linalool, and (S)-(1)-linalool
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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either Mg2+ or Mn2+ is required for activity, the optimum is 5 mM Mg2+
Mn2+
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either Mg2+ or Mn2+ is required for activity, the optimum is 0.25 mM Mg2+
additional information
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no enzyme activity in the presence of Ca2+, Cd2+, Co2+, Cu2+, Ni2+, and Zn2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
(2E,6E)-farnesyl diphosphate
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20 mM MgCl2, 0.2 mM MnCl2, 0.2 mM NaWO4, and 0.1 mM NaF, pH not specified in the publication, at 30°C
0.0009
geranyl diphosphate
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20 mM MgCl2, 0.2 mM MnCl2, 0.2 mM NaWO4, and 0.1 mM NaF, pH not specified in the publication, at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 8.2
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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highest expression
Manually annotated by BRENDA team
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ear leaf
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63960
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calculated from amino acid sequence
66000
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gel filtration
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Econopac 10DG column chromatography and Strep-Tactine affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E391Q
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the mutation is located in the vicinity of the catalytic center but does not influence enzymatic activity
E455V
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the mutation results in an increase of catalytic activity
I479T
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the mutation is located in the vicinity of the catalytic center but does not influence enzymatic activity
K402Q
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the mutation is located in the vicinity of the catalytic center but does not influence enzymatic activity
T383S
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the mutation is located in the vicinity of the catalytic center but does not influence enzymatic activity
W163R
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the mutation restores much of the wild type activity (albeit maintaining the increased concentration of (E)-beta-farnesene relative to that of sesquithujene and (S)-beta-bisabolene)
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.3.101)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)