Affordable Access

Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.

Publication Date
  • Research Article
  • Biology


Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC and the C-terminal domain of Pseudomonas putida creatinase (EC are related. A detailed comparison of the three-dimensional folds of the two enzymes confirms this homology: with an approximately 260-residue chain segment, 218 C alpha atoms of the structures superimpose within 2.5 A; only 41 of these overlapping positions (i.e., 19%) feature identical amino acids in the two protein chains. Notwithstanding this striking correspondence in structure, methionine aminopeptidase binds and is stimulated by Co2+, while creatinase is not a metal-dependent enzyme. Searches of protein data banks using sequence and structure-based profiles reveal other enzymes, including aminopeptidase P (EC, prolidase (EC, and agropine synthase, that likely share the same "pita-bread" fold common to creatinase and methionine aminopeptidase.

There are no comments yet on this publication. Be the first to share your thoughts.