Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.3.22 - germacradienol synthase and Organism(s) Streptomyces avermitilis and UniProt Accession Q82L49

for references in articles please use BRENDA:EC4.2.3.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.22 germacradienol synthase
IUBMB Comments
Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate . Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16 geosmin synthase), a widely occurring metabolite of many streptomycetes, bacteria and fungi . Also catalyses the reaction of EC 4.2.3.75, (-)-germacrene D synthase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces avermitilis
UNIPROT: Q82L49
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Streptomyces avermitilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
terpene cyclase, germacrene d synthase, spterp13, germacradienol/geosmin synthase, germacradienol synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
germacradienol/germacrene D synthase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol-forming]
Requires Mg2+ for activity. H-1si of farnesyl diphosphate is lost in the formation of (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol. Formation of (-)-germacrene D involves a stereospecific 1,3-hydride shift of H-1si of farnesyl diphosphate. Both products are formed from a common intermediate [2]. Other enzymes produce germacrene D as the sole product using a different mechanism. The enzyme mediates a key step in the biosynthesis of geosmin (see EC 4.1.99.16 geosmin synthase), a widely occurring metabolite of many streptomycetes, bacteria and fungi [2]. Also catalyses the reaction of EC 4.2.3.75, (-)-germacrene D synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
211049-88-6
-
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 + H2O
(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate
show the reaction diagram
-
66%
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
10-20% activity, compared to reaction with Mg2+
Cu2+
10-20% activity, compared to reaction with Mg2+
Fe2+
50% activity, compared to reaction with Mg2+
Mn2+
10-20% activity, compared to reaction with Mg2+
Zn2+
50% activity, compared to reaction with Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000075
farnesyl diphosphate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031
farnesyl diphosphate
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83000
determined by SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Q-Sepharose resin and a Q-Sepharose column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for construction of a geoA-deletion mutant of Streptomyces avermitilis, and for expression in Escherichia coli BL21DE3 cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
resuspended inclusion body protein is refolded
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cane, D.E.; He, X.; Kobayashi, S.; Omura, S.; Ikeda, H.
Geosmin biosynthesis in Streptomyces avermitilis. Molecular cloning, expression, and mechanistic study of the germacradienol/geosmin synthase
J. Antibiot.
59
471-479
2006
Streptomyces avermitilis (Q82L49), Streptomyces avermitilis
Manually annotated by BRENDA team