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Human liver mitochondrial aldehyde dehydrogenase: Three‐dimensional structure and the restoration of solubility and activity of chimeric forms
The structure of the human mitochondrial enzyme was solved and it was found to be identical to the beef enzyme, suggesting that to have a soluble or active enzyme a favorable interaction must occur between a residue in a surface loop and a residue elsewhere in the molecule even though neither make contact with the active site region of the enzyme. Expand
Structural and Functional Consequences of Coenzyme Binding to the Inactive Asian Variant of Mitochondrial Aldehyde Dehydrogenase
The data presented shows that Glu-487 maintains a critical function in linking the structure of the coenzymebinding site to that of the active site through its interactions with Arg-264 and Arg-475, and in doing so, creates the stable structural scaffold conducive to catalysis. Expand
The N‐terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly
The N‐terminal segment of the mature protein, and not the presequence, makes a major contribution to the folding, assembly, and stability of the precursor and may play a role in folding and hence the translocation of thePriority ALDH1 proved to be more stable against urea denaturation than ALDH2. Expand
Structure-based antigenic epitope and PEGylation improve the efficacy of staphylokinase
The present study suggests that site mutant P EGylation, PEG-Sak-C104R, is a suitable type of PEGylation for clinical applications and further optimization would help maintain the bioactivity and decrease the immunogenicity of staphylokinase. Expand
Cleavage of pro-tumor necrosis factor alpha by ADAM metallopeptidase domain 17: a fluorescence-based protease assay cleaves its natural protein substrate.
A fluorescence-based Adam 17 activity assay that cleaves pro-tumor necrosis factor alpha (pro-TNFα) protein substrate has been developed and was able to identify the inhibitor binding to substrate protein in addition to that binding to the protease itself. Expand