Family C69
Summary for family C69
Family type peptidase | C69.001 - dipeptidase A (Lactobacillus helveticus), MEROPS Accession MER0002163 (peptidase unit: 6-474) |
Content of family | Peptidase family C69 contains dipeptidases and aminopeptidases. |
History |
Identifier created: MEROPS 6.5 (22 December 2003)
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Catalytic type | Cysteine |
Active site residues | C6 |
Active site | Catalytic residues were tentatively identified by sequence comparison with penicillin V acylase (C59.001) and other N-terminal nucleophile hydrolases (Pei & Grishin, 2003). The alignments highlighted the conservation of two regions of hydrophobic residues located between the catalytic Cys and the conserved Arg/Lys and Asp residues (see the Alignment). |
Activities and specificities | It has been demonstrated that dipeptidase A (C69.001) is able to cleave Leu Leu and Phe Leu, but not Leu-Leu-NH2 and Phe-Leu-NH2, indicating that the enzyme can only cleave dipeptides with a free C-terminus (Dudley & Steele, 2004). The peptidase is also unable to cleave bonds involving proline (Vesanto et al., 1996). |
Inhibitors | Dipeptidase A (C69.001) is inhibited by p-hydroxymercuribenzoate (Vesanto et al., 1996). |
Molecular structure | No three-dimensional structure is available for any member of the family. The molecular mass of native dipeptidase A was estimated to be 420 kDa and the monomeric mass deduced as 53.5 kDa, suggesting that dipeptidase A is an octamer (Vesanto et al., 1996). |
Clan | PB |
Subclan | PB(C) |