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On the Mechanism of Action of Urocanase: Observation of the Enzyme‐Bound NAD + ‐Inhibitor Adduct by 13 C NMR Spectroscopy
Author(s) -
Schubert Carsten,
Röttele Herbert,
Spraul Manfred,
Rétey János
Publication year - 1995
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199506521
Subject(s) - adduct , nad+ kinase , chemistry , enzyme , stereochemistry , nuclear magnetic resonance spectroscopy , biochemistry , organic chemistry
Not the aromatic form 1 a but the nonaromatic form 1b of the enzyme‐inhibitor complex is preferred at the active site of urocanase. This can be observed in situ with 13 C‐labeled components by NMR spectroscopy. The enzyme‐bound adducts were characterized by use of (4‐ 13 C)NAD + ‐containing urocanase and the labeled inhibitor (5′‐ 13 C)imidazolepropionate. • = 13 C, R = adenosine diphosphate ribosyl.