MAs can be synthesized by a conserved pathway begin with trimerization of three molecular of S-adenosyl-L-methionine into nicotianamine (NA) by nicotianamine synthase (NAS) [ 6], and then NA is converted into 2′-deoxymugineic acid (DMA), the precursor of MAs, by nicotianamine aminotransferase (NAAT) [ 7] and deoxymugineic acid synthase (DMAS) [ 8].
The substrate is activated through protonation by a conserved tyrosine.
Figure 4 shows a conserved complex predicted by our pipeline.
A series of semi-batch polymerization runs catalyzed by a trimerization catalyst bis 2-dodecylsulfanyl-ethyl)amine-CrCl3 and a copolymerization catalyst Et(Ind)2ZrCl2 in toluene at 74∘C were carried out to verify the model.
Here, we present the crystal structure of the P. aeruginosa enzyme and show that it adopts a trimeric structure, partly held together by an immunoglobulin-like trimerization domain that is C-terminal to a classical β-propeller sialidase domain.
Macroautophagy is an evolutionarily conserved intracellular degradation system used by life ranging from yeasts to mammals.
We have recently reported the in vitro and in vivo properties of multivalent antibodies generated by fusing a trimerization (TIE) domain to the N- or C-terminus of a single-chain variable fragment (scFv) (Sánchez-Arevalo Lobo et al. 2006; Cuesta et al. 2009, 2012; Blanco-Toribio et al. 2013).
In this study, recombinant BLyS/APRIL heterotrimers were produced by using a novel trimerization domain, purified, and extensively characterized.
Normal transient diffusion, featured by an exponent 1/2, conserves half of energy, while anomalous diffusion, featured by an exponent p different from 1/2, conserves only 100 p%.
*As determined by InterProScan and NCBI conserved domains search.
