Literature summary for 4.2.3.21 extracted from

Mathis, J.R.; Back, K.; Starks, C.; Noel, J.; Poulter, C.D.; Chappell, J.
Pre-steady-state study of recombinant sesquiterpene cyclases (1997), Biochemistry, 36, 8340-8348.

Search for more literature for 4.2.3.21

Cloned(Commentary)

Cloned (Comment)	Organism
hexahistidyl-tagged enzyme expressed in Escherichia coli, genes for vetispiradiene synthase, a chimeric 5-epi-aristolochene synthase and a chimeric sesquiterpene cyclase possessing multifunctional epi-aristolochene and vetispiradiene activity	Hyoscyamus muticus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.002	0.005	trans,trans-farnesyl diphosphate	native enzyme	Hyoscyamus muticus
0.0035	-	trans,trans-farnesyl diphosphate	recombinant enzyme	Hyoscyamus muticus

Organism

Organism	UniProt	Comment	Textmining
Hyoscyamus muticus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant vetispiradiene synthase, a chimeric 5-epi-aristolochene synthase and a chimeric sesquiterpene cyclase possessing multifunctional epi-aristolochene and vetispiradiene activity	Hyoscyamus muticus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
trans,trans-farnesyl diphosphate	mechanism involves an initial rapid equilibrium of enzyme with substrate to form an enzyme-substrate complex, followed by a slower conversion of farnesyl diphosphate to an enzyme-bound hydrocarbon, and a subsequent rate-limiting step	Hyoscyamus muticus	vetispiradiene + diphosphate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.04	-	trans,trans-farnesyl diphosphate	recombinant enzyme	Hyoscyamus muticus

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Release 2023.1 (January 2023)