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• W4256005745 abstract "Abstract Many peptide hormones and neuropeptides require an amidated carboxy terminal for full biological activity. This reaction is carried out in two steps: hydroxylation of a C‐terminal glycine and cleavage of the C N bond with the release of glyoxylate. The enzyme peptidyl‐α‐hydroxyglycine α‐amidating lyase (PAL; EC 4.3.2.5) catalyzes the second step of this reaction, N ‐dealkylation of the peptidyl‐α‐hydroxyglycine to generate the α‐amidated peptide and glyoxylate. The X‐ray crystal structure of the PAL catalytic core (PALcc), alone and in complex with the nonpeptidic substrate α‐hydroxyhippuric acid, shows that PAL folds as a six‐bladed β‐propeller. The active site is formed by a Zn 2+ ion coordinated by three histidine residues; the substrate binds to this site with its α‐hydroxyl group coordinated to the Zn 2+ ion. A tyrosine residue (Tyr654) at the active site acts as the catalytic base for hydroxyl deprotonation, an unusual role for tyrosine residue. In the reaction mechanism, proposed on the basis of the structure and validated by biochemical analysis of site‐directed PALcc mutants, the substrate α‐hydroxyl that coordinates the catalytic Zn 2+ directly is deprotonated by Tyr654. The generation of the required tyrosinate is aided by an arginine residue that, together with the Zn 2+ , lowers the p K a of the catalytic tyrosine." @default.
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• W4256005745 date "2004-03-05" @default.
• W4256005745 modified "2023-09-26" @default.
• W4256005745 title "Peptidyl‐α‐Hydroxyglycine α‐Amidating Lyase ( <scp>PAL</scp> )" @default.
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• W4256005745 doi "https://doi.org/10.1002/0470028637.met282" @default.
• W4256005745 hasPublicationYear "2004" @default.
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