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- ******************************************************
- * Aminopeptidase P and proline dipeptidase signature *
- ******************************************************
-
- Aminopeptidase P (EC 3.4.11.9) is the enzyme responsible for the release of
- any N-terminal amino acid adjacent to a proline residue. Proline dipeptidase
- (EC 3.4.13.9) (prolidase) splits dipeptides with a prolyl residue in the
- carboxyl terminal position.
-
- Escherichia coli aminopeptidase P II (gene pepP) [1], Escherichia coli proline
- dipeptidase (gene pepQ) [2], and Human proline dipeptidase (gene PEPD) [3] are
- evolutionary related. These proteins are manganese metalloenzymes.
-
- As a signature pattern for these enzymes we selected a conserved region that
- contains three histidine residues.
-
- -Consensus pattern: H-G-[LIVM]-[SG]-H-x-L-G-[LIVM]-x-V-H-D
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: May 1991 / First entry.
-
- [ 1] Yoshimoto T., Tone H., Honda T., Osatomi K., Kobayashi R., Tsuru D.
- J. Biochem. 105:412-416(1989).
- [ 2] Nakahigashi K., Inokuchi H.
- Nucleic Acids Res. 18:6439-6439(1990).
- [ 3] Endo F., Tanoue A., Nakai H., Hata A., Indo Y., Titani K., Matsuda I.
- J. Biol. Chem. 264:4476-4481(1989).
-