Background: Protein glutaminase (PG) catalyzes deamination of Gln residues in proteins. Results: The structures of mature and pro forms and a pro form mutant reveal that the side chain of Gln-47 of mutant A47Q mimics the protein substrate of PG. Conclusion: Gln-47 of A47Q forms an S-acyl covalent intermediate with the catalytic Cys. Significance: PG shares a common catalytic mechanism with transglutaminase and cysteine protease.

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Page s136 s136 systems, thus the inactive dimer conformation may be the keypoint in determining signaling specifity.

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