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Literature summary for 5.5.1.13 extracted from

  • Hayashi, K.; Kawaide, H.; Notomi, M.; Sakigi, Y.; Matsuo, A.; Nozaki, H.
    Identification and functional analysis of bifunctional ent-kaurene synthase from the moss Physcomitrella patens (2006), FEBS Lett., 580, 6175-6181.
    View publication on PubMed
Search for more literature for 5.5.1.13

Cloned(Commentary)

Cloned (Comment) Organism
expression as myc-fusion protein using Spodoptera frugiperda 21 insect cells. Sequence contains a DVDD motif responsible for copalyl diphosphate synthase activity and a DDYFD motif responsible for ent-kaurene synthase activity Physcomitrium patens

Protein Variants

Protein Variants Comment Organism
additional information 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 Physcomitrium patens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
101000
-
 x * 101000, calculated, x * 106000, SDs-PAGE of myc-fusion protein Physcomitrium patens
106000
-
 x * 101000, calculated, x * 106000, SDs-PAGE of myc-fusion protein Physcomitrium patens

Organism

Organism UniProt Comment Textmining
Physcomitrium patens
-
 bifunctional copalyl diphosphate synthase/ent-kaurene synthase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
copalyl diphosphate bifunctional copalyl diphosphate synthase/ent-kaurene synthase Physcomitrium patens ent-16-alpha-hydroxy-kaurene + ent-kaurene + diphosphate 86% and 14%, resp. ?
geranylgeranyl diphosphate
-
 Physcomitrium patens copalyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 101000, calculated, x * 106000, SDs-PAGE of myc-fusion protein Physcomitrium patens