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Carbamylation of N-terminal proline.

ABSTRACT: Protein carbamylation is of great concern both in vivo and in vitro. Here, we report the first structural characterization of a protein carbamylated at the N-terminal proline. The unexpected carbamylation of the ?-amino group of the least reactive codified amino acid has been detected in high-resolution electron density maps of a new crystal form of the HIV-1 protease/saquinavir complex. The carbamyl group is found coplanar to the proline ring with a trans conformation. The reaction of N-terminal with cyanate ion derived from the chaotropic agent urea was confirmed by mass spectra analysis on protease single crystals. Implications of carbamylation process in vitro and in vivo are discussed.

SUBMITTER: Olajuyigbe FM

PROVIDER: S-EPMC4007797 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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Carbamylation of N-terminal proline.

Olajuyigbe Folasade M FM Demitri Nicola N Ajele Joshua O JO Maurizio Elisa E Randaccio Lucio L Geremia Silvano S

ACS medicinal chemistry letters 20100602 6

Protein carbamylation is of great concern both in vivo and in vitro. Here, we report the first structural characterization of a protein carbamylated at the N-terminal proline. The unexpected carbamylation of the α-amino group of the least reactive codified amino acid has been detected in high-resolution electron density maps of a new crystal form of the HIV-1 protease/saquinavir complex. The carbamyl group is found coplanar to the proline ring with a trans conformation. The reaction of N-termina ...[more]

PMID: 24900204

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