Enzymes utilizing glutamine as an amide donor

Amide nitrogen from glutamine is a major source of nitrogen atoms incorporated biosynthetically into other amino acids, purine and pyrimidine bases, amino-sugars, and coenzymes. A family comprised of at least sixteen amidotransferases are known to catalyze amide nitrogen transfer from glutamine to t...

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Bibliographic Details
Published inAdvances in enzymology and related subjects Vol. 72; p. 87
Main Authors Zalkin, H, Smith, J L
Format Journal Article
LanguageEnglish
Published United States 1998
Subjects
Allosteric Regulation
Amides - metabolism
Carbon-Nitrogen Ligases - metabolism
Gene Expression Regulation, Enzymologic
Glutamine - metabolism
Humans
Models, Molecular
Transferases - metabolism
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Summary:Amide nitrogen from glutamine is a major source of nitrogen atoms incorporated biosynthetically into other amino acids, purine and pyrimidine bases, amino-sugars, and coenzymes. A family comprised of at least sixteen amidotransferases are known to catalyze amide nitrogen transfer from glutamine to their acceptor substrates. Recent fine structural advances, largely as a result of X-ray crystallography, now provide structure-based mechanisms that help to explain fundamental aspects of the catalytic and regulatory interactions of several of these aminotransferases. This chapter provides an overview of this recent progress made on the characterization of amidotransferase structure and mechanism.
ISSN:0065-258X