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Literature summary for 2.5.1.89 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene ape_1385, recombinant expression in Escherichia coli strain BL21 (DE3) Aeropyrum pernix

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inhibition Aeropyrum pernix

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ about 10% of the activity with Mg2+ Aeropyrum pernix
Cu2+ about 5% of the activity with Mg2+ Aeropyrum pernix
Mg2+ required Aeropyrum pernix
Mn2+ about 20% of the activity with Mg2+ Aeropyrum pernix

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
all-trans-geranylfarnesyl diphosphate + 6 isopentenyl diphosphate Aeropyrum pernix
-
6 diphosphate + hexatrans,tetracis-undecaprenyl diphosphate
-
?
all-trans-geranylfarnesyl diphosphate + 6 isopentenyl diphosphate Aeropyrum pernix DSM 11879
-
6 diphosphate + hexatrans,tetracis-undecaprenyl diphosphate
-
?
additional information Aeropyrum pernix the undecaprenyl diphosphate synthase from Aeropyrum pernix that has anomalous substrate specificity, due to the fact that only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate for the archaeal enzyme ?
-
?
additional information Aeropyrum pernix DSM 11879 the undecaprenyl diphosphate synthase from Aeropyrum pernix that has anomalous substrate specificity, due to the fact that only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate for the archaeal enzyme ?
-
?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YC66 gene ape_1385
-
Aeropyrum pernix DSM 11879 Q9YC66 gene ape_1385
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
all-trans-geranylfarnesyl diphosphate + 6 isopentenyl diphosphate
-
Aeropyrum pernix 6 diphosphate + hexatrans,tetracis-undecaprenyl diphosphate
-
?
all-trans-geranylfarnesyl diphosphate + 6 isopentenyl diphosphate
-
Aeropyrum pernix 6 diphosphate + hexatrans,tetracis-undecaprenyl diphosphate i.e. (Z,Z,Z,Z,Z,Z,E,E,E,E)-UPP [(2Z,6Z,10Z,14Z,18Z,22Z,26E,30E,34E,38E)-3,7,11,15,19,23,27,31,35,39,43-undecamethyl-2,6,10,14,18,22,26,30,34,38,42-tetratetracontaundecaen-1-yl diphosphate] ?
all-trans-geranylfarnesyl diphosphate + 6 isopentenyl diphosphate
-
Aeropyrum pernix DSM 11879 6 diphosphate + hexatrans,tetracis-undecaprenyl diphosphate
-
?
additional information the undecaprenyl diphosphate synthase from Aeropyrum pernix that has anomalous substrate specificity, due to the fact that only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate for the archaeal enzyme Aeropyrum pernix ?
-
?
additional information the enzyme is a cis-prenyltransferas, determination of substrate specificity, product chain-length, and cofactor requirement, overview. The most preferred allylic substrates are farnesyl diphosphate and geranylfarnesyl diphosphate, the main product is UPP, regardless of the substrate. When the ratio of IPP to geranylfarnesyl diphosphate is decreased to 1, the UPP synthase predominately yields shorter C30-45 products. When the ratio is increased to 100, the main product is C60 dodecaprenyl diphosphate. The chain-length of the product of UPP synthase, which determines the structure of the glycosyl carrier lipid, is variable depending on the substrate ratio in the cells of Aeropyrum pernix. A 10fold increase in the substrate ratio results in a significant rise in the production of all-trans-hexaprenyl diphosphate. No activity with dimethylallyl diphosphate. The enzyme also shows the activity of hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific], EC 2.5.1.82, and of geranylgeranyl diphosphate synthase, EC 2.5.1.29 Aeropyrum pernix ?
-
?
additional information the undecaprenyl diphosphate synthase from Aeropyrum pernix that has anomalous substrate specificity, due to the fact that only dimethylallyl diphosphate and geranylfarnesyl diphosphate, both of which are unusual substrates for known cis-prenyltransferases, are likely available as an allylic primer substrate for the archaeal enzyme Aeropyrum pernix DSM 11879 ?
-
?
additional information the enzyme is a cis-prenyltransferas, determination of substrate specificity, product chain-length, and cofactor requirement, overview. The most preferred allylic substrates are farnesyl diphosphate and geranylfarnesyl diphosphate, the main product is UPP, regardless of the substrate. When the ratio of IPP to geranylfarnesyl diphosphate is decreased to 1, the UPP synthase predominately yields shorter C30-45 products. When the ratio is increased to 100, the main product is C60 dodecaprenyl diphosphate. The chain-length of the product of UPP synthase, which determines the structure of the glycosyl carrier lipid, is variable depending on the substrate ratio in the cells of Aeropyrum pernix. A 10fold increase in the substrate ratio results in a significant rise in the production of all-trans-hexaprenyl diphosphate. No activity with dimethylallyl diphosphate. The enzyme also shows the activity of hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific], EC 2.5.1.82, and of geranylgeranyl diphosphate synthase, EC 2.5.1.29 Aeropyrum pernix DSM 11879 ?
-
?

Synonyms

Synonyms Comment Organism
undecaprenyl diphosphate synthase
-
Aeropyrum pernix

Temperature Optimum [°C]

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

pH Optimum

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