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Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases
Author(s) -
Sorci Leonardo,
Brunetti Lucia,
Cialabrini Lucia,
Mazzola Francesca,
Kazanov Marat D.,
D'Auria Sabato,
Ruggieri Silverio,
Raffaelli Nadia
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.063
Subject(s) - amidohydrolase , serine , chemistry , biochemistry , hydrolase , enzyme , substrate specificity , nicotinamide mononucleotide , stereochemistry , nad+ kinase , nicotinamide adenine dinucleotide
NMN deamidase (PncC) is a bacterial enzyme involved in NAD biosynthesis. We have previously demonstrated that PncC is structurally distinct from other known amidohydrolases. Here, we extended PncC characterization by mutating all potential catalytic residues and assessing their individual roles in catalysis through kinetic analyses. Inspection of these residues’ spatial arrangement in the active site, allowed us to conclude that PncC is a serine‐amidohydrolase, employing a Ser/Lys dyad for catalysis. Analysis of the PncC structure in complex with a modeled NMN substrate supported our conclusion, and enabled us to propose the catalytic mechanism.