2.5.1.83: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]

This is an abbreviated version!
For detailed information about hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], go to the full flat file.

Reaction

Synonyms

C30PP synthase, COQ1, Coq1p, EC 2.5.1.33, hexaprenyl pyrophosphate synthetase, hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], HexPP synthase, HexPPs, HexPS

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.83 hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
84	AA Sequence
1	CAS Registry Number
2	Cloned(Commentary)
1	Crystallization (Commentary)
6	Inhibitors
12	KM Value [mM]
2	Localization
3	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
67	Organism
3	Pathway
8	Protein Variants
3	Purification (Commentary)
3	Reaction
21	Reference
31	Substrates and Products (Substrate)
6	Subunits
19	Synonyms
1	Systematic Name
1	Temperature Stability [°C]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 2.5.1.83 - hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure both in the substrate-free form and in complex with 7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate ammonium salt, an analog of farnesyl diphosphate, to 2.5 A and 2.7 A resolution, respectively. The structure of subunit HexB is composed of mostly antiparallel alpha-helices joined by connecting loops. Two aspartate-rich motifs and the other characteristic motifs in HexB are located around the diphosphate part of 7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate. Despite the very low amino acid sequence identity and the distinct polypeptide chain lengths between subunits HexA and HexB, the structure of HexA is quite similar to that of HexB. The aliphatic tail of 7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate is accommodated in a large hydrophobic cleft starting from HexB and penetrating to the inside of HexA suggesting that HexB catalyzes the condensation reactions and that HexA is directly involved in the product chain length control in cooperation with HexB

Micrococcus luteus

O66129; O66127

722728