EC Number   |
Substrates |
Products |
Reversibility |
|---|
   3.4.99.B2 | D-Asp-L-Ala-L-Glu-L-Phe-L-Arg-L-His-D-Asp-L-Ser-Gly-L-Tyr + H2O |
- |
? |
- |
? |
| 3.4.99.B2 | DAEFRH-(D-Asp)-GSY + H2O |
synthetic Abeta peptide. No cleavage of the D-Aspcontaining Abeta peptide, paenidase I and II. Paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side |
DAEFRH-(D-Asp) + GSY |
- |
? |
| 3.4.99.B2 | L-Thr-L-Val-L-Leu-D-alpha-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg + H2O |
- |
? |
- |
? |
| 3.4.99.B2 | more |
the enzyme may serve as a scavenger against accumulation of racemized proteins in aging |
? |
- |
? |
| 3.4.99.B2 | more |
the accumulation of D-isomers of aspartic acid in proteins during aging is involved in the pathogenesis of Alzheimers disease, cataracts, and arteriosclerosis. The enzyme may serve as a scavenger against accumulation of racemized proteins in aging |
? |
- |
? |
| 3.4.99.B2 | more |
no activity with: acetyl-L-Asp-p-nitroanilide, D-Asp-p-nitroanilide, A-Ala-p-nitroanilide, D-Leu-p-nitroanilide, D-Phe-p-nitroanilide, L-Asp-p-nitroanilide, L-Ala-p-nitroanilide, L-Leu-p-nitroanilide, L-Phe-p-nitroanilide, L-Arg-p-nitroanilide, L-Glu-p-nitroanilide, Gly-p-nitroanilide, L-His-p-nitroanilide, L-Ile-p-nitroanilide, L-Lys-p-nitroanilide, L-Met-p-nitroanilide, L-Pro-p-nitroanilide, L-Val-p-nitroanilide, p-nitroanilide, succinyl-L-Ala-L-Pro-L-Ala, succinyl-L-Ala-L-Ala-L-Ala-p-nitroanilide, L-Pyr-p-nitroanilide, Arg-4-methylcoumaryl-7-amide, benzoyl-Arg-4-methylcoumaryl-7-amide, tert-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide, Pro-Phe-Arg-4-methylcoumaryl-7-amide, acetyl-Tyr-val-Ala-Asp-4-methylcoumaryl-7-amide, acetyl-ASp-GLu-Val-Asp-4-methylcoumaryl-7-amide, acetyl-Val-Glu-Ile-Asp-4-methylcoumaryl-7-amide |
? |
- |
? |
| 3.4.99.B2 | more |
no activity with acetyl-Tyr-Val-Ala-Asp-4-methylcoumaryl-7-amide, acetyl-Asp-Glu-Val-Asp-4-methylcoumaryl-7-amide, succinyl-Gly-Pro-Leu-Gly-Pro-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide, Leu-4-methylcoumaryl-7-amide, succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Leu-Leu-Glu-4-methylcoumaryl-7-amide, Ala-Ala-Phe-4-methylcoumaryl-7-amide, succinyl-Ala-[D-Ser]-4-methylcoumaryl-7-amide, succinyl-[D-Ser]-4-methylcoumaryl-7-amide |
? |
- |
? |
| 3.4.99.B2 | more |
no activity with succinyl-L-Asp-7-amido-4-methylcoumarin, L-Thr-L-Val-L-Leu-L-alpha-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg, L-Thr-L-Val-L-Leu-D-beta-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg and L-Thr-L-Val-L-Leu-D-beta-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg |
? |
- |
? |
| 3.4.99.B2 | more |
enzyme specifically recognizes an internal D-Asp residue to cleave [D-Asp]-X peptide bonds |
? |
- |
? |
| 3.4.99.B2 | succinyl-D-Asp-4-methylcoumaryl-7-amide + H2O |
paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side |
succinyl-D-Asp + 7-amino-4-methylcoumarin |
- |
? |
