Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities.

Saccharomyces cerevisiae Thi20 is a fusion protein with homology to Bacillus subtilis ThiD and TenA. The N-terminus of Thi20 has significant sequence homology to B. subtilis ThiD, while the C-terminus has homology to B.

Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II.

Bacillus subtilis gene products TenA and TenI have been implicated in regulating the production of extracellular proteases, but their role in the regulation process remains unclear. The structural characterization of these proteins was undertaken to help provide insight into their function. We have determined the structure of TenA alone and in complex with 4-amino-2-methyl-5-hydroxymethylpyrimidine, and we demonstrate that TenA is a thiaminase II.

N-terminal extensions of the human AMPD2 polypeptide influence ATP regulation of isoform L.

Human tissues and cells express three AMP deaminase (AMPD) isoforms containing divergent N-terminal domains, and each member of the multigene family encoding these enzymes produces alternative transcripts that confer additional N-terminal divergence through extensions and cassette-type substitutions. Available data suggest that divergent N-terminal domains can influence AMPD isoform behavior, but the functional significance for additional divergence within each enzyme is unknown. Three isoform L (AMPD2) variants, 1A/2, 1B/2, and 1B/3, contain N-terminal extensions of 47, 128, and 53 amino acids, respectively.

Expression, purification, and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes.

AMP deaminase (AMPD) is a multigene family in higher eukaryotes whose three members encode tetrameric isoforms that catalyze the deamination of AMP to IMP. AMPD polypeptides share conserved C-terminal catalytic domains of approximately 550 amino acids, whereas divergent N-terminal domains of approximately 200-330 amino acids may confer isoform-specific properties to each enzyme. However, AMPD polypeptides are subject to limited N-terminal proteolysis during purification and subsequent storage at 4 degrees C.