Literature summary for 2.5.1.31 extracted from

Chang, S.Y.; Tsai, P.C.; Tseng, C.S.; Liang, P.H.
Refolding and characterization of a yeast dehydrodolichyl diphosphate synthase overexpressed in Escherichia coli (2001), Protein Expr. Purif., 23, 432-439.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli. Thioredoxin and His tag are utilized to increase the solubility of the recombinant protein and facilitate its purification using Ni-nitrilotriacetic acid column	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.027	-	isopentenyl diphosphate	-	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	the recombinant enzyme expressed in Escherichia coli mostly exists in pellet in the absence of detergents, a low quantity of soluble enzyme is purified	Saccharomyces cerevisiae	-	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Saccharomyces cerevisiae	the synthesized long-chain dehydrodolichyl diphosphate serves as a precursor of glycosyl carrier in glycoprotein biosynthesis in eukaryotes	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharomyces cerevisiae

Renatured (Commentary)

Renatured (Comment)	Organism
the recombinant protein in the pellet is solubilized with 7 M urea and purified using nickel-nitrilotriacetic acid under denaturing conditions. The protein refolding is achieved via the stepwise dialysis to remove the denaturant in the presence of 6 mM beta-mercaptoethanol. Alternatively, on-column refolding is carried out in a single step to obtain the active protein in large quantities. beta-Mercaptoethanol and Triton are both required in this quick refolding process	Saccharomyces cerevisiae

Renatured (Comment)

Organism

the recombinant protein in the pellet is solubilized with 7 M urea and purified using nickel-nitrilotriacetic acid under denaturing conditions. The protein refolding is achieved via the stepwise dialysis to remove the denaturant in the presence of 6 mM beta-mercaptoethanol. Alternatively, on-column refolding is carried out in a single step to obtain the active protein in large quantities. beta-Mercaptoethanol and Triton are both required in this quick refolding process

Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
isopentenyl diphosphate + farnesyl diphosphate	-	Saccharomyces cerevisiae	C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate	the C55 polymer is the major product in presence of Triton X-100, without Triton C55-C75 polyprenyl diphosphates are generated	?
additional information	the synthesized long-chain dehydrodolichyl diphosphate serves as a precursor of glycosyl carrier in glycoprotein biosynthesis in eukaryotes	Saccharomyces cerevisiae	?	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Saccharomyces cerevisiae
0.0002	-	isopentenyl diphosphate	-	Saccharomyces cerevisiae