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

BRENDA support

Literature summary for 1.3.1.83 extracted from

  • Xu, Q.; Eguchi, T.; Mathews, I.I.; Rife, C.L.; Chiu, H.J.; Farr, C.L.; Feuerhelm, J.; Jaroszewski, L.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Weekes, D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
    Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids (2010), J. Mol. Biol., 404, 403-417.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining

General Information

General Information Comment Organism
evolution highly conserved regions of characterized geranylgeranyl reductases, GGRs, from archaea, plants, and bacteria, overview Thermoplasma acidophilum
additional information structural basis for recognition of a geranyl group by geranylgeranyl reductases, GGRs, overview Thermoplasma acidophilum
physiological function DGGR catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions Thermoplasma acidophilum