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The identification of a reactive lysine residue in lobster glyceraldehyde-3-phosphate dehydrogenase.

Lobster glyceraldehyde-3-phosphate dehydrogenase was found to contain a reactive lysine residue that is specifically acetylated when the NAD-deficient form of the enzyme is incubated with [1-14C]acetyl phosphate at pH 8.5. The residue was identified by sequence analysis as number 182 in the polypeptide chain of the enzyme. 
 
 
 
Both the acetylation behaviour and the position of the lysine residue are identical with that found for mammalian glyceraldehyde-3-phosphate dehydrogenases. In addition the amino acid sequence around lysine 182 was found to be identical, except for a few conservative changes, with the corresponding sequence in pig glyceraldehyde-3-phosphate dehydrogenase.