Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases-Reference-Cited by-同舟云学术

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Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases

Published:2014-02-11 Issue:6 Volume:588 Page:1016-1023
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sorci Leonardo,Brunetti Lucia,Cialabrini Lucia,Mazzola Francesca,Kazanov Marat D.,D'Auria Sabato,Ruggieri Silverio,Raffaelli Nadia

Funder

Italian Ministry of Foreign Affairs

Direzione Generale per la Promozione del Sistema Paese

Montalcini International Program Grant

Italian Ministry of Education, University, and Research

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference37 articles.

1. Structural and catalytic diversity within the amidohydrolase superfamily;Seibert;Biochemistry,2005

2. Design of potent aspartic protease inhibitors to treat various diseases;Nguyen;Arch. Pharm. (Weinheim),2008

3. Catalytic triads and their relatives;Dodson;Trends Biochem. Sci,1998

4. An alternative mechanism for amidase signature enzymes;Labahn;J. Mol. Biol,2002

5. Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad;Shin;J. Biol. Chem,2003

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1. Periplasmic binding proteins Bug69 and Bug27 from Bordetella pertussis are in vitro high‐affinity quinolinate binders with a potential role in NAD biosynthesis;FEBS Open Bio;2024-08-08

2. Characterization of Two NMN Deamidase Mutants as Possible Probes for an NMN Biosensor;International Journal of Molecular Sciences;2021-06-13

3. Characterization and mutational analysis of a nicotinamide mononucleotide deamidase from Agrobacterium tumefaciens showing high thermal stability and catalytic efficiency;PLOS ONE;2017-04-07

4. A new cross-linked enzyme aggregate biocatalyst for NAD+-booster production;RSC Advances;2017

5. A putative low-molecular-mass penicillin-binding protein (PBP) of Mycobacterium smegmatis exhibits prominent physiological characteristics of dd-carboxypeptidase and beta-lactamase;Microbiology;2015-05-01

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