Literature summary for 2.5.1.B35 extracted from

Mori, T.; Ogawa, T.; Yoshimura, T.; Hemmi, H.
Substrate specificity of undecaprenyl diphosphate synthase from the hyperthermophilic archaeon Aeropyrum pernix (2013), Biochem. Biophys. Res. Commun., 436, 230-234.

Search for more literature for 2.5.1.B35

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Aeropyrum pernix

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	5 mM, complete inhibition	Aeropyrum pernix

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	a divalent metal ion is necessary for the activity. Ca2+, Mn2+ and Cu2+ all confer significantly lower activity than Mg2+ does	Aeropyrum pernix
Cu2+	a divalent metal ion is necessary for the activity. Ca2+, Mn2+ and Cu2+ all confer significantly lower activity than Mg2+ does	Aeropyrum pernix
Mg2+	a divalent metal ion is necessary for the activity. The addition of 5 mM Mg2+ gives the highest activity within the conditions tested. A 10fold higher concentration of Mg2+ continues to show activity that is comparable to 5 mM Mg2+	Aeropyrum pernix
Mn2+	a divalent metal ion is necessary for the activity. Ca2+, Mn2+ and Cu2+ all confer significantly lower activity than Mg2+ does	Aeropyrum pernix

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
geranylfarnesyl diphosphate + 6 isopentenyl diphosphate	Aeropyrum pernix	the enzyme is involved in the biosynthetic pathway for isoprenoid compounds	6 diphosphate + tetratrans,hexacis-undecaprenyl diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Aeropyrum pernix	Q9YC66	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Aeropyrum pernix

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate	about 95% of the activity with geranylfarnesyl diphosphate. The main product is undecaprenyl diphosphate, regardless of the substrate. If the ratio of IPP to the allylic substrate becomes lower, the product will be shorter, probably because of the shortage of isopentenyl diphosphate or because of the frequent dissociation of an intermediate from the active site by competitive binding of the hydrophobic allylic substrate	Aeropyrum pernix	8 diphosphate + ditrans,octacis-undecaprenyl diphosphate	the stereochemistry of the product is not experimentally determined	?
geranyl diphosphate + 9 isopentenyl diphosphate	about 65% of the activity with geranylfarnesyl diphosphate. The main product is undecaprenyl diphosphate, regardless of the substrate. If the ratio of IPP to the allylic substrate becomes lower, the product will be shorter, probably because of the shortage of isopentenyl diphosphate or because of the frequent dissociation of an intermediate from the active site by competitive binding of the hydrophobic allylic substrate	Aeropyrum pernix	9 diphosphate + monotrans,nonacis-undecaprenyl diphosphate	the stereochemistry of the product is not experimentally determined	?
geranylfarnesyl diphosphate + 6 isopentenyl diphosphate	the enzyme is involved in the biosynthetic pathway for isoprenoid compounds	Aeropyrum pernix	6 diphosphate + tetratrans,hexacis-undecaprenyl diphosphate	-	?
geranylfarnesyl diphosphate + 6 isopentenyl diphosphate	geranylfarnesyl diphosphate is the most preferred allylic substrate. The main product is undecaprenyl diphosphate, regardless of the substrate. If the ratio of isopentenyl diphosphate to the allylic substrate becomes lower, the product will be shorter, probably because of the shortage of isopentenyl diphosphate or because of the frequent dissociation of an intermediate from the active site by competitive binding of the hydrophobic allylic substrate	Aeropyrum pernix	6 diphosphate + tetratrans,hexacis-undecaprenyl diphosphate	the stereochemistry of the product is not experimentally determined	?
geranylgeranyl diphosphate + 7 isopentenyl diphosphate	about 45% of the activity with geranylfarnesyl diphosphate. The main product is undecaprenyl diphosphate, regardless of the substrate. If the ratio of IPP to the allylic substrate becomes lower, the product will be shorter, probably because of the shortage of isopentenyl diphosphate or because of the frequent dissociation of an intermediate from the active site by competitive binding of the hydrophobic allylic substrate. When the ratio of isopentenyl diphosphate to geranylfarnesyl diphosphate is decreased to 1, the UPP synthase predominately yields shorter C3045 products	Aeropyrum pernix	7 diphosphate + tritrans,heptacis-undecaprenyl diphosphate	the stereochemistry of the product is not experimentally determined	?
additional information	dimethylallyl diphosphate does not react with the enzyme. If the ratio of IPP to the allylic substrate becomes lower, the product will be shorter, probably because of the shortage of isopentenyl diphosphate or because of the frequent dissociation of an intermediate from the active site by competitive binding of the hydrophobic allylic substrate	Aeropyrum pernix	?	-	?

Synonyms

Synonyms	Comment	Organism
ape_1385	locus name	Aeropyrum pernix
undecaprenyl diphosphate synthase	ambiguous	Aeropyrum pernix
UPP synthase	-	Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
60	-	assay at	Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
90	-	1 h, the enzyme retains more than 80% of its activity	Aeropyrum pernix
100	-	1 h, complete inactivation	Aeropyrum pernix

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Aeropyrum pernix

General Information

General Information	Comment	Organism
physiological function	the enzyme is involved in the biosynthetic pathway for isoprenoid compounds	Aeropyrum pernix

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Release 2023.1 (January 2023)