Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.30 extracted from

  • Suzuki, T.; Zhang, Y.W.; Koyama, T.; Sasaki, D.Y.; Kurihara, K.
    Direct observation of substrate-enzyme complexation by surface forces measurement (2006), J. Am. Chem. Soc., 128, 15209-15214.
    View publication on PubMed
Search for more literature for 2.5.1.30

Cloned(Commentary)

Cloned (Comment) Organism
the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ this enzyme is composed of two dissociable subunits that exhibit a catalytic activity only when they are associated together in the presence of a cofactor, Mg2+, and a substrate, farnesyl diphosphate. The quartz-crystal microbalance measurement reveals that farnesyl diphosphate is preferentially bound to subunit II in the presence of Mg2+, while the atomic force microscopy measurement shows that the adhesive force between the subunits is observed only in the presence of both Mg2+ and farnesyl diphosphate Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P31112 and P31114 P31112: subunit 1, P31114: subunit 2
-

Purification (Commentary)

Purification (Comment) Organism
the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex Bacillus subtilis 4 diphosphate + all-trans-heptaprenyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
dimer this enzyme is composed of two dissociable subunits that exhibit a catalytic activity only when they are associated together in the presence of a cofactor, Mg2+, and a substrate, farnesyl diphosphate. The quartz-crystal microbalance measurement reveals that farnesyl diphosphate is preferentially bound to subunit II in the presence of Mg2+, while the atomic force microscopy measurement shows that the adhesive force between the subunits is observed only in the presence of both Mg2+ and farnesyl diphosphate Bacillus subtilis

Synonyms

Synonyms Comment Organism
HepPP synthase
-
 Bacillus subtilis