Literature summary for 4.2.3.19 extracted from

Kawaide, H.; Hayashi, K.; Kawanabe, R.; Sakigi, Y.; Matsuo, A.; Natsume, M.; Nozaki, H.
Identification of the single amino acid involved in quenching the ent-kauranyl cation by a water molecule in ent-kaurene synthase of Physcomitrella patens (2011), FEBS J., 278, 123-133.

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Protein Variants

Protein Variants	Comment	Organism
A710C	no change in reaction product profile compared to wild-type	Physcomitrium patens
A710F	mutant converts geranylgeranyl diphosphate to ent-kaurene as the sole product	Physcomitrium patens
A710G	no change in reaction product profile compared to wild-type	Physcomitrium patens
A710M	mutant converted geranylgeranyl diphosphate to ent-kaurene as the sole product	Physcomitrium patens
A710N	no change in reaction product profile compared to wild-type	Physcomitrium patens
A710S	no change in reaction product profile compared to wild-type	Physcomitrium patens
additional information	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	Physcomitrium patens
additional information	construction of chimeric proteins of Physcomitrella patens PpCPS/KS with Jungermannia subulata, the chimeric cyclases Pp131-566 /Js574-86 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	Liochlaena subulata

Organism

Organism	UniProt	Comment	Textmining
Liochlaena subulata	-	bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19	-
Physcomitrium patens	A5A8G0	bifunctional ent-copalyl diphosphate synthase EC 5.5.1.13, and ent-kaurene synthase, EC 4.2.3.19	-

Reaction

Reaction	Comment	Organism	Reaction ID
ent-copalyl diphosphate = ent-kaurene + diphosphate	the determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides	Liochlaena subulata	a
ent-copalyl diphosphate = ent-kaurene + diphosphate	the hydrophobicity and size of the side chain residue at the bifunctional CPS/KS amino acid 710 is responsible for quenching the ent-kauranyl cation by the addition of a water molecule. The determination of the final products of CPS/KSs in bryophytes depends on the sequence and structure of the C-terminal regions of CPS/KSs. Thus, the type A cyclization reaction of both PpCPS/KS and JsCPS /KS occurs near the C-terminal region of the polypeptides	Physcomitrium patens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ent-copalyl diphosphate	-	Physcomitrium patens	ent-kaurene + diphosphate	the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate	?
ent-copalyl diphosphate	-	Liochlaena subulata	ent-kaurene + diphosphate	the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate	?
ent-copalyl diphosphate + H2O	-	Physcomitrium patens	16alpha-hydroxy-ent-kaurane + diphosphate	the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate	?
ent-copalyl diphosphate + H2O	-	Liochlaena subulata	16alpha-hydroxy-ent-kaurane + diphosphate	the bifunctional ent-kaurene synthase produces both entkaurene and 16alpha-hydroxy-ent-kaurane from geranylgeranyl diphosphate via ent-copalyl diphosphate	?

Synonyms

Synonyms	Comment	Organism
CPS/KS	-	Physcomitrium patens
CPS/KS	-	Liochlaena subulata

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Release 2023.1 (January 2023)