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NMR Studies of the Interaction of Tryparedoxin with Redox-Inactive Substrate Homologues †

✍ Scribed by Krumme, Dirk; Budde, Heike; Hecht, Hans-Jürgen; Menge, Ulrich; Ohlenschläger, Oliver; Ross, Anton; Wissing, Josef; Wray, Victor; Flohé, Leopold

Book ID
127186932
Publisher
American Chemical Society
Year
2003
Tongue
English
Weight
725 KB
Volume
42
Category
Article
ISSN
0006-2960

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A rapid and sensitive method is described for determining the activity of alanine racemase (5. I. I. I) with its substrates. Alanine racemase from Bacillus subtilis catalyzes the exchange of the (Y hydrogen of L and D alanine, a racemic mixture of alanine as we!! as both the Q hydrogens of glycine w