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Information on EC 4.2.3.19 - ent-kaurene synthase and Organism(s) Phaeosphaeria sp. and UniProt Accession O13284

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.19 ent-kaurene synthase
IUBMB Comments
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
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This record set is specific for:
Phaeosphaeria sp.
UNIPROT: O13284
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Word Map
The taxonomic range for the selected organisms is: Phaeosphaeria sp.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ent-kaurene synthase, ppcps/ks, kaurene synthase, cps/ks, ent-kaurene synthase b, bifunctional cps/ks, ent-kaur-16-ene synthase, ent-copalyldiphosphate synthase/ent-kaurene synthase, copalyl diphosphate/kaurene synthase, class i ditps ent-kaurene synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ent-kaurene synthase B
-
-
-
-
ent-kaurene synthetase B
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-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
-
-
-
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diphosphate lysis
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-
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-
SYSTEMATIC NAME
IUBMB Comments
ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming)
Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase)
CAS REGISTRY NUMBER
COMMENTARY hide
9055-64-5
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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
ent-copalyl diphosphate
ent-kaurene + diphosphate
show the reaction diagram
ent-copalyl diphosphate
ent-kaurene + diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ent-copalyl diphosphate
ent-kaurene + diphosphate
show the reaction diagram
involved in biosynthesis of gibberellins
-
?
ent-copalyl diphosphate
ent-kaurene + diphosphate
show the reaction diagram
involved in biosynthesis of gibberellins
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-isopropyl-4'(trimethylammonium chloride)-5'-methylphenyl piperidine-1-carboxylate
Amo-1618
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
SDS-PAGE, cloned fusion protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D132A
low activity
D320A
low activity
D656A
no activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 as glutathione-S-transferase fusion protein, enzyme shows EC 4.2.3.19 and EC 5.5.1.13 activity
in Escherichia coli as glutathione-S-transferase fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawaide, H.; Imai, R.; Sassa, T.; Kamiya, Y.
ent-Kaurene synthetase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis
J. Biol. Chem.
272
21706-21712
1997
Phaeosphaeria sp. (O13284), Phaeosphaeria sp., Phaeosphaeria sp. L487 (O13284)
Manually annotated by BRENDA team
Kawaide, H.; Sassa, T.; Kamiya, Y.
Functional analysis of the two interacting cyclase domains in ent-kaurene synthase from the fungus Phaeosphaeria sp. L487 and a comparison with cyclases from higher plants
J. Biol. Chem.
275
2276-2280
2000
Phaeosphaeria sp. (O13284), Phaeosphaeria sp., Phaeosphaeria sp. L487 (O13284)
Manually annotated by BRENDA team