Literature summary for 2.5.1.58 extracted from

Su, P.; Gao, L.; Liu, S.; Guan, H.; Wang, J.; Zhang, Y.; Zhao, Y.; Hu, T.; Tu, L.; Zhou, J.; Ma, B.; Liu, X.; Huang, L.; Gao, W.
Probing the function of protein farnesyltransferase in Tripterygium wilfordii (2019), Plant Cell Rep., 38, 211-220 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	the two subunits have the same cytoplasmic localization pattern	Tripterygium wilfordii	5737	-

Organism

Organism	UniProt	Comment	Textmining
Tripterygium wilfordii	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	lowest expression level found	Tripterygium wilfordii	-
additional information	ubiquitous expression of both subunits in all sampled organ tissues, with the highest transcription levels in root bark and the lowest in leaf	Tripterygium wilfordii	-
root	root bark, highest expression level	Tripterygium wilfordii	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
farnesyl diphosphate + N-dansyl-GCVLS	-	Tripterygium wilfordii	S-farnesyl-N-dansyl-GCVLS + diphosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	1 * 38600, alpha-subunit, and 1 * 50800, beta-subunit, calulated from sequence	Tripterygium wilfordii

pI Value

Organism	Comment	pI Value Maximum	pI Value
Tripterygium wilfordii	beta-subunit, calulated from sequence	-	5.3
Tripterygium wilfordii	alpha-subunit, calculated from sequence	-	5.4

General Information

General Information	Comment	Organism
physiological function	dimerization of subunits alpha and beta is required for farnesylation activity	Tripterygium wilfordii

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Release 2023.1 (January 2023)