Results 21 to 30 of about 621 (94)

The cis‐prenyltransferase protein family in Taraxacum koksaghyz

The Plant Journal, Volume 121, Issue 3, February 2025.
Significance Statement The novelty of this work lies in the comprehensive description of cis‐prenyl transferases in the rubber‐producing plant Taraxacum koksaghyz. This provides valuable insights for breeding and rational protein design in heterologous systems.
Boje Müller, Eva Niephaus, Wolfgang Eisenreich, Jan Niklas Bröker, Richard M. Twyman, Dirk Prüfer, Christian Schulze Gronover   +6 more
wiley   +1 more source

Purification and characterization of a polyisoprenyl phosphate phosphatase from pig brain. Possible dual specificity.

The Journal of biological chemistry, 1998
Microsomal fractions from pig and calf brain catalyze the enzymatic dephosphorylation of endogenous and exogenous dolichyl monophosphate (Dol-P) (Sumbilla, C. A., and Waechter, C. J. (1985) Methods Enzymol. 111, 471-482). The Dol-P phosphatase (EC 3.1.3.51) has been solubilized by extracting pig brain microsomes with the nonionic detergent Nonidet P-40
D W, Frank, C J, Waechter
openaire   +1 more source

Structure-Function Analysis of Enzymes of the Polyisoprenyl-Phosphate Hexose-1-Phosphate Transferase family [PDF]

, 2011
Enzymes of the polyisoprenyl-phosphate hexose-1-phosphate transferase (PHPT) family are integral membrane proteins that initiate the synthesis of glycans by catalyzing the transfer of a hexose-1-phosphate sugar from UDP-hexose to the lipid carrier undecaprenyl phosphate (Und-P).
openaire  

Structure-Function Analysis of UDP-Sugar: Polyisoprenyl Phosphate Sugar-1-Phosphate Transferases [PDF]

, 2013
The synthesis of lipid-linked glycans is a conserved process in eukaryotes and prokaryotes that is initiated by two major enzyme families: the polyisoprenyl-phosphate hexose-1-phosphate transferases (PHPTs) and the polyisoprenyl-phosphate N-acetylaminosugar-1-phosphate transferases (PNPTs). These enzymes contain multiple membrane domains and transfer a
openaire  

Purification and Characterization of a Polyisoprenyl Phosphate Phosphatase from Pig Brain [PDF]

Journal of Biological Chemistry, 1998
David W. Frank, Charles J. Waechter
openaire   +1 more source

Glycoprotein biosynthesis: studies on thyroid mannosyltransferases. II. Characterization of a polyisoprenyl mannosyl phosphate and evaluation of its intermediary role in the glycosylation of exogenous acceptors.

The Journal of biological chemistry, 2006
The transfer of mannose from GDP-mannonse to exogenous glycopeptides and simple glycosides has been shown to be carried out by calf thyroid particles (Adamany, A. M., and Spiro, R. G. (1975) J. Biol. Chem. 250, 2830-2841). The present investigation indicates that this mannosylation process is accomplished through two sequential enzymatic reactions. The
A M, Adamany, R G, Spiro
openaire   +1 more source

A Family of Antibiotics That Evades Resistance by Binding Polyprenyl Phosphates. [PDF]

ACS Infect Dis, 2023
Rosenzweig AF, Wang Z, Morales-Amador A, Spotton K, Brady SF.   +4 more
europepmc   +1 more source

Real-Time Tracking of Intracellular Prenyl Phosphate Pools in the Marine Diatom <i>Phaeodactylum tricornutum</i> with a Metabolite Protein-Based Biosensor. [PDF]

ACS Synth Biol
Patwari P, Moses T, Arnspang EC, Fabris M.   +3 more
europepmc   +1 more source

Dimerization-Dependent Trans-Domain Coupling Enables Intermediate Transfer in Fungal Haloacid Dehalogenase-Like Terpene Cyclases. [PDF]

J Am Chem Soc
Chen TH, Huang KF, Chou TH, Tseng CC, Huang RJ, Ko TP, Liang SY, Chein RJ, Lin HC.   +8 more
europepmc   +1 more source

Air microbial sampling in operating theatres by active and passive methods: equation correlation from the GISIO-ISChIA study results and comparison with the EU GGMP recommendation, towards the definition of threshold values. [PDF]

Acta Biomed, 2023
Pasquarella CIM, Auxilia F, Barchitta M, Cristina ML, D'Alessandro D, Mura I, Nobile M, Veronesi L, Albertini R, Agodi A.   +9 more
europepmc   +1 more source