Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold.
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C-terminal domain of Pseudomonas putida creatinase (EC 3.5.3.3) 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 3.4.11.9), prolidase (EC 3.4.13.9), and agropine synthase, that likely share the same "pita-bread" fold common to creatinase and methionine aminopeptidase.
Bazan
J F
JF
Institute of Molecular Biology, Howard Hughes Medical Institute, Eugene, OR.
Weaver
L H
LH
Roderick
S L
SL
Huber
R
R
Matthews
B W
BW
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry*; D004150:Dipeptidases / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D063208:Methionyl Aminopeptidases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D014512:Ureohydrolases / Q000737:chemistry*
D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases; C022750:X-Pro aminopeptidase; D004150:Dipeptidases; C022449:proline dipeptidase; D014512:Ureohydrolases; C019944:creatinase