Crystallization of NAD+ synthetase fromBacillus subtilis

✍ Scribed by Rizzi, Menico; Nessi, Claudio; Bolognesi, Martino; Coda, Alessandro; Galizzi, Alessandro

• Book ID: 101228430
• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 240 KB
• Volume: 26
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199610)26:2<236::aid-prot12>3.0.co;2-q

✦ Synopsis

NAD+-synthetase is a ubiquitous enzyme catalyzing the last step in the biosynthesis of NAD+. Mutants of NAD+ synthetase with impaired cellular functions have been isolated, indicating a key role for this enzyme in cellular metabolism. Crystals of the enzyme from Bacillus subtilis suitable for x-ray crystallographic investigation have been grown from polyethylene glycol solutions. Investigation on the structural organization of NAD+ synthetase, a n enzyme fundamental for NAD+ biosynthesis, and belonging to the recently characterized amidotransferase enzymatic family, will provide more insight into the catalytic mechanism of deamido-NAD+ + NAD+ conversion, a biosynthetic process that is a potential target for the development of antibiotic compounds against Bacillus sp. and related bacteria.