Results 231 to 240 of about 21,027 (334)

Evolutionary divergence and functional insights into the heteromeric cis‐prenyltransferase of Paramecium tetraurelia

open access: yesThe FEBS Journal, EarlyView.
Heteromeric cis‐prenyltransferases (CPT) are indispensable for dolichol synthesis and protein N‐glycosylation in most eukaryotes. The catalytic subunits are strongly conserved throughout evolution, in contrast to the evolutionarily variable accessory subunits. The POC1 protein from Paramecium tetraurelia is the smallest identified CPT‐accessory subunit
Agnieszka Onysk   +8 more
wiley   +1 more source

Structural analysis of the NifL‐NifA complex reveals the molecular basis of anti‐activation of nitrogen fixation gene expression in Azotobacter vinelandii

open access: yesThe FEBS Journal, EarlyView.
Using cryo‐EM combined with biochemical and genetic approaches, we mapped the interaction surface between NifL and NifA to gain insights into the regulation of nitrogen fixation genes in A. vinelandii. Our findings suggest that NifL, a homolog of histidine kinases lacking phosphorylation activity, evolved to act as a steric block of NifA activity ...
Marcelo Bueno Batista   +6 more
wiley   +1 more source

Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in substrate-bound forms. [PDF]

open access: yesActa Crystallogr F Struct Biol Commun
Titterington JA   +6 more
europepmc   +1 more source

Cytidine Diphosphate-Ribitol Analysis for Diagnostics and Treatment Monitoring of Cytidine Diphosphate-l-Ribitol Pyrophosphorylase A Muscular Dystrophy [PDF]

open access: bronze, 2019
Walinka van Tol   +15 more
openalex   +1 more source

Expanding the substrate scope of a bacterial monoterpene synthase for the production of sesquiterpenoid and diterpenoid products

open access: yesThe FEBS Journal, EarlyView.
We have converted the only known true bacterial monoterpene synthase, cineole synthase from Streptomyces clavuligerus (bCinS, C10 substrate), to a highly competent sesquiterpene synthase (C15) with a minimum number of rational mutations. By comparison with diterpene synthases (C20), we were then able to bestow diterpene synthase activity on bCinS. This
Nicole G. H. Leferink   +3 more
wiley   +1 more source

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