Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.
Keywords:
Acetyltransferases
,Binding Sites
,Glutamic Acid
,Models, Molecular
,Mycobacterium tuberculosis
,Ornithine
,Streptomyces
,Substrate Specificity
