5.5.1.13: ent-copalyl diphosphate synthase
This is an abbreviated version!
For detailed information about ent-copalyl diphosphate synthase, go to the full flat file.
Word Map on EC 5.5.1.13
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5.5.1.13
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gibberellin
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diterpene
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diterpenoids
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geranylgeranyl
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phytohormone
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phytoalexins
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ent-cpp
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ent-kaurenoic
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phytocassanes
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e,e,e-geranylgeranyl
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oscps4
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3-oxidase
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ga-deficient
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labdane-related
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ga1
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ditpss
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oryzalexins
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ga20ox
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syn-copalyl
- 5.5.1.13
- gibberellin
-
diterpene
-
diterpenoids
-
geranylgeranyl
-
phytohormone
-
phytoalexins
-
ent-cpp
-
ent-kaurenoic
-
phytocassanes
-
e,e,e-geranylgeranyl
-
oscps4
-
3-oxidase
-
ga-deficient
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labdane-related
- ga1
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ditpss
-
oryzalexins
- ga20ox
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syn-copalyl
Reaction
Synonyms
copalyl diphosphate synthase/ent-kaurene synthase, copalyl synthase/kaurene synthase, CPS, CPS/KS, CPS1, CPS2, CPS2/Cyc2, CPS3, ent-copalyl/ent-kaurene synthase, ent-copylyl diphosphate synthase/ent-kaurene synthase, ent-CPS, ent-kaurene synthase A, ent-kaurene synthetase A, GfCPS/KS, OsCPS1, OsCPS1ent, OsCPS2ent, OsCyc2
ECTree
Advanced search results
Engineering
Engineering on EC 5.5.1.13 - ent-copalyl diphosphate synthase
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T421A
the mutant exhibits a 163fold reduction in kcat (KM is increased 2fold)
A710C
A710F
A710G
A710L
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the substitution changes the ratio of ent-kaurene and 16alpha-hydroxy-entkaurane produced. The production of ent-kaurene is increased to the same level as that of 16alpha-hydroxyent-kaurane
A710M
A710N
A710S
C717A
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site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
additional information
A710C
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site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
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mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710F
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site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
A710G
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site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
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mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product
A710M
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site-directed mutagenesis, the mutant protein shows the same enzymic activity as wild-type Jungermannia subulata JsCPS/KS
A710N
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site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
A710S
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site-directed mutagenesis, the mutant shows unaltered activity and reaction product profile compared to the wild-type Jungermannia subulata JsCPS/KS
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construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
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Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity
additional information
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sequence contains a DVDD motif responsible for copalyl diphosphate synthase activity and a DDYFD motif responsible for ent-kaurene synthase activity. Mutation of DVDD motif to AVAD leads to loss of function, mutation of DDYFD motif to AAYFD results in accumulation of ent-copalyl diphosphate
additional information
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construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-886 and Pp131-504 /Js512-886 and produce only ent-kaurene. Chimeric cyclases, Pp131-622 /Js630-886 and Pp131-714 /Js722-886, lose all enzymic activity
additional information
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Jungermannia subulata JsCPS/KS peptide fragments are replaced by the corresponding Physcomitrella patens PpCPS/KS region. A PCR-amplified Jungermannia subulata JsCPS/KS DNA fragment corresponding to amino acids 574-746 is replaced by Physcomitrella patens PpCPS/KS amino acids 566-740. Four chimeric cyclases, Physcomitrella patens Pp566/Js574-746/Pp740, Pp566/Js574-721/Pp715, Pp627/Js635-721/Pp715, and Pp666/Js674-721/Pp715, have enzymic activity and produce only ent-kaurene from geranylgeranyl diphosphate, like Jungermannia subulata JsCPS/KS. The chimeric cyclase Pp566/Js574-634/Pp628 shows the same activity as wild-type PpCPS/KS, converting geranylgeranyl diphosphate to both ent-kaurene and 16alpha-hydroxy-ent-kaurane. Overview mutant chimeric constructs and enzymatic activity