Information on EC 5.5.1.17 - (S)-beta-macrocarpene synthase

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The expected taxonomic range for this enzyme is: Zea mays

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EC NUMBER
COMMENTARY hide
5.5.1.17
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RECOMMENDED NAME
GeneOntology No.
(S)-beta-macrocarpene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-beta-bisabolene = (S)-beta-macrocarpene
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
zealexin biosynthesis
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Sesquiterpenoid and triterpenoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(S)-beta-macrocarpene lyase (decyclizing)
The synthesis of (S)-beta-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-beta-bisabolene (cf. EC 4.2.3.55, (S)-beta-bisabolene synthase). The second step is the isomerization to (S)-beta-macrocarpene.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme may be involved in plant defense; the enzyme may be involved in plant defense
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-beta-bisabolene
(S)-beta-macrocarpene
show the reaction diagram
geranyl diphosphate
(S)-beta-bisabolene + (S)-beta-macrocarpene
show the reaction diagram
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in the presence of geranylgeranyl diphosphate, TPS11 also catalyzes the formation of beta-myrcene and linalool, along with minor amounts of limonene, alpha-thujene, sabinene, and alpha-terpinolene
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?
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
(S)-beta-bisabolene
(S)-beta-macrocarpene
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the enzyme is mostly stimulated by 10 mM Mg2+; the enzyme is mostly stimulated by 10 mM Mg2+; TPS6 requires a divalent metal ion, with Mg2+ and Mn2+ being effective, optimum activity with 5 mM Mg2+ and 5 mM Mn2+. Although the Km for Mn2+ is significantly lower than for Mg2+, the enzyme is more likely to operate with a Mg2+ cofactor in planta, because the concentration of Mg2+ in plant cells is about 2 orders of magnitudes higher than Mn2+. In the presence of Mn2+, the product spectrum of TPS6 is shifted toward an increased production of (S)-beta-bisabolene and a decreased production of (S)-beta-macrocarpene. KM-value for Mg2+ measured with 0.01 mM farnesyl diphosphate: 0.131 mM
Mn2+
the enzyme is stimulated by 0.25 mM Mn2+. In the presence of Mn2+, there is increased formation of (S)-beta-bisabolene; the enzyme is stimulated by 0.25 mM Mn2+. In the presence of Mn2+, there is increased formation of (S)-beta-bisabolene; TPS6 requires a divalent metal ion, with Mg2+ and Mn2+ being effective, optimum activity with 5 mM Mg2+ and 5 mM Mn2+. Although the Km for Mn2+ is significantly lower than for Mg2+, the enzyme is more likely to operate with a Mg2+ cofactor in planta, because the concentration of Mg2+ in plant cells is about 2 orders of magnitudes higher than Mn2+. In the presence of Mn2+, the product spectrum of TPS6 is shifted toward an increased production of (S)-beta-bisabolene and a decreased production of (S)-beta-macrocarpene. KM-value for Mn2+ measured with 0.01 mM farnesyl diphosphate: 0.0234 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
geranyl diphosphate
recombinant enzyme, in the presence of 0.05 mM Mn2+, pH and temperature not specified in the publication; recombinant enzyme, in the presence of 0.05 mM Mn2+, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
forming beta-macrocarpene; forming beta-macrocarpene; in presence of 5 mM Mg2+
8.5
forming beta-bisabolene; forming beta-bisabolene
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.6
half-maximal activity at pH 6.2 and at pH 8.6, in presence of 5 mM Mg2+. Within a pH range from 5.0 to 8.0, the major product is (S)-beta-macrocarpene, but higher pH values favor the formation of (S)-beta-bisabolene
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is predominantly active in the roots; the enzyme is predominantly active in the roots
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial; partial; partial purification; partial purification
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Top10 cells; expressed in Escherichia coli Top10 cells; overexpression in Escherichia coli; overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after leaf damage by Spodoptera littoralis, the transcript level of TSP11 is elevated; after leaf damage by Spodoptera littoralis, the transcript level of TSP6 is elevated
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D526N
inactive; inactive; mutation inactivates the enzyme completely
Y522F
the mutation strongly reduces the rate of reprotonation of (S)-beta-bisabolene; the mutation strongly reduces the rate of reprotonation of (S)-beta-bisabolene
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LINKS TO OTHER DATABASES (specific for EC-Number 5.5.1.17)
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)