Zo-peroxidase: Crystal structure and sequence of a highly-glycosylated peroxidase resistant to high concentrations of HO from Japanese radish.

Understanding Peroxidase (PRXs) enzymatic diversity and functional significance from a three-dimensional point of view is a key point for structural and mechanistic studies. In this context, Zo-peroxidase (ZoPrx) a member of the class III peroxidases and secreted by plants, differs from all previously described PRXs because of its remarkable catalytic stability in the presence of hydrogen peroxide. In this work, we present the crystallographic structure of ZoPrx isolated from Japanese radish, at 2.

Solution structure of 6aJL2 and 6aJL2-R24G amyloidogenics light chain proteins.

AL amyloidosis is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light chain amyloid fibers in different organs, causing organ failure. The immunoglobulin light chain germinal line 6a has been observed to over-express in AL patients, moreover, it was observed that, out of these amyloidogenic proteins, 25% present a mutation of an Arg to Gly in position 24. In vitro studies have shown that this mutation produces proteins with a higher amyloid fiber propensity.

(1)H, (15)N and (13)C resonance assignments for 3rC and 3rCWP: amyloidogenic variants of imunoglobulin λ 3 light-chain.

Primary amyloidosis (AL) is the most common amyloid systemic disease and it is characterized by the deposition of immunoglobulin light-chain amyloid fibers in different organs, causing organ failure. The germ-line lambda 3 immunoglobulin light-chain proteins have been correlated with the AL condition. Two mutants have been derived from this germ-line, the single mutant C34Y (3rC) and the triple mutant C34Y, W35A and P7D (3rCWP), presenting a remarkable difference in amyloid fibril formation propensities in vitro.