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Crystallization of NAD + synthetase from Bacillus subtilis
Author(s) -
Rizzi Menico,
Nessi Claudio,
Bolognesi Martino,
Coda Alessandro,
Galizzi Alessandro
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199610)26:2<236::aid-prot12>3.0.co;2-q
Subject(s) - nad+ kinase , bacillus subtilis , enzyme , biochemistry , biosynthesis , bacteria , chemistry , biology , genetics
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, an 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. © 1996 Wiley‐Liss, Inc.