Information on EC 4.1.99.16 - geosmin synthase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.99.16
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RECOMMENDED NAME
GeneOntology No.
geosmin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O = (-)-geosmin + acetone
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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geosmin biosynthesis
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Sesquiterpenoid and triterpenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
germacradienol geosmin-lyase (acetone forming)
Requires Mg2+. Geosmin is the cause of the characteristic smell of moist soil. It is a bifunctional enzyme. The N-terminal part of the enzyme is EC 4.2.3.22, germacradienol synthase, and forms germacradienol from FPP. The C-terminal part of the enzyme catalyses the conversion of germacradienol to geosmin via (1S,4aS,8aS)-1,4a-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. ANA318, isolated at the Australian Water Quality Centre in 1995 from a sample sourced from Pejar Dam in Goulburn, NSW, Australia, during a taste and odor episode
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Manually annotated by BRENDA team
i.e. ANA318, isolated at the Australian Water Quality Centre in 1995 from a sample sourced from Pejar Dam in Goulburn, NSW, Australia, during a taste and odor episode
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Manually annotated by BRENDA team
germacradienol/geosmin synthase
UniProt
Manually annotated by BRENDA team
C-terminal domain; germacradienol/germacrene D synthase
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O
(-)-geosmin + acetone
show the reaction diagram
catalysed by the C-terminal domain of the bifunctional enzyme
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?
(2E,6E)-farnesyl diphosphate + H2O
(4S,7R)-germacra-1(10)E,5E-diene-11-ol + (7S)-germacrene D + geosmin + ?
show the reaction diagram
overall reaction of germacradienol/geosmin synthase
presence of Mg2+, synthesis of 66% (4S,7R)-germacra-1(10)E,5E-diene-11-ol, 24% (7S)-germacrene D, 8% geosmin, and 2% of a hydrocarbon, tentatively assigned the structure of octalin
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?
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
10-20% of the activity with Mg2+
Cu2+
10-20% of the activity with Mg2+
Fe2+
50% of the activity with Mg2+
Mg2+
preferred divalent cation, maximum activity at 10 mM
Mn2+
10-20% of the activity with Mg2+
Zn2+
50% of the activity with Mg2+
additional information
absolute requirement for a divalent cation. No activity with Ni2+ or Ca2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000075
(2E,6E)-farnesyl diphosphate
pH 8.2, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031
(2E,6E)-farnesyl diphosphate
Streptomyces avermitilis
Q82L49
pH 8.2, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
relative enzyme expression analysis
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