Literature summary for 4.2.3.61 extracted from

Diaz, J.E.; Lin, C.S.; Kunishiro, K.; Feld, B.K.; Avrantinis, S.K.; Bronson, J.; Greaves, J.; Saven, J.G.; Weiss, G.A.
Computational design and selections for an engineered, thermostable terpene synthase (2011), Protein Sci., 20, 1597-1606.

Search for more literature for 4.2.3.61

Cloned(Commentary)

Cloned (Comment)	Organism
-	Nicotiana tabacum

Protein Variants

Protein Variants	Comment	Organism
additional information	engineering of a thermostable mutant by SCADS algorithm to suggest mutations based on side-chain interactions consistent with the nearby protein backbone, neighboring sidechains, and the local environment, and by replacement of solvent-exposed hydrophobic residues and the addition of salt bridges on the surface of the mutant enzyme. Contrary to wild-type, mutant is still active to 65°C but produces additional sesquiterpene products	Nicotiana tabacum

Organism

Organism	UniProt	Comment	Textmining
Nicotiana tabacum	Q40577	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate	-	Nicotiana tabacum	(+)-5-epiaristolochene + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
5EAT	-	Nicotiana tabacum

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
40	-	wild-type, no activity above	Nicotiana tabacum
65	-	thermostable mutant, active up to	Nicotiana tabacum

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
38	-	wild-type, denaturation	Nicotiana tabacum
83	-	thermostable mutant, denaturation	Nicotiana tabacum

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Release 2023.1 (January 2023)