Structural insights into the reaction mechanism of S-adenosyl-L-homocysteine hydrolase.

S-adenosyl-L-homocysteine hydrolase (SAH hydrolase or SAHH) is a highly conserved enzyme that catalyses the reversible hydrolysis of SAH to L-homocysteine (HCY) and adenosine (ADO). High-resolution crystal structures have been reported for bacterial and plant SAHHs, but not mammalian SAHHs. Here, we report the first high-resolution crystal structure of mammalian SAHH (mouse SAHH) in complex with a reaction product (ADO) and with two reaction intermediate analogues-3'-keto-aristeromycin (3KA) and noraristeromycin (NRN)-at resolutions of 1.

Crystallization of mouse S-adenosyl-L-homocysteine hydrolase.

S-adenosyl-L-homocysteine hydrolase (SAHH; EC 3.3.1.

cDNA cloning and life-cycle stage-specific expression of coronin from Physarum polycephalum.

Coronin cDNA was cloned from the plasmodia of Physarum polycephalum. The amino acid sequence deduced from the cDNA was comprised of 449 residues and showed 60% identity to that of Dictyostelium discoideum coronin. Southern blot analysis suggested that the coronin gene present in the P.

[The relationship between extracranial carotid atherosclerosis in an ultrasound study and periventricular hyperintensity in MR images].

We have evaluated the relationship between carotid atherosclerotic change and periventricular hyper intensity (PVH). PVH was studied in 66 cases with cerebral thrombosis, comparing them with another group of age-matched controls, which consisted of 29 cases with hypertension, diabetes, and hypercholesteremia. MRI (fluid attenuated inversion recovery) and B-mode carotid ultrasonography of each lesion were analyzed.