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Histidine in Enzyme Active Centers
Author(s) -
Schneider Friedhelm
Publication year - 1978
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.197805831
Subject(s) - histidine , imidazole , chemistry , residue (chemistry) , active site , active center , stereochemistry , nucleophile , catalysis , enzyme catalysis , enzyme , hydrogen bond , side chain , molecule , organic chemistry , polymer
The presence of histidine in the active center of an enzyme can be demonstrated by kinetic measurements, chemical modification, NMR spectroscopy or X‐ray structure analysis. Histidine is the only naturally occurring amino acid to contain an imidazole residue as a side chain. The role of histidine in enzyme catalysis depends, inter alia , upon the special features of the imidazole residue: it thus tends to form hydrogen bonds, combines donor and acceptor properties and can take part in either nucleophilic or base catalysis. In some of these enzymes the position of each atom is known; however, the theories as to how the catalysis proceeds at a molecular level are controversial.