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Literature summary for 3.4.22.16 extracted from

  • Brümme, D.; Bescherer, K.; Kirschke, H.; Fittkau, S.
    Enzyme-substrate interactions in the hydrolysis of peptides by cathepsins B and H from rat liver (1987), Biochem. J., 245, 381-385.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.7
-
succinyl-Ala-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
0.7
-
succinyl-Ala-Ala-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
2.9
-
succinyl-Pro-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
3
-
succinyl-Ala-Pro-Ala-4-nitroanilide
-
Rattus norvegicus
3.5
-
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro-NH2
-
Rattus norvegicus
7
-
succinyl-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
7.4
-
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro
-
Rattus norvegicus
10.2
-
succinyl-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
27.8
-
succinyl-Ala-Ala-Pro-4-nitroanilide
-
Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Proteins + H2O Rattus norvegicus rather broad specificity of aminopeptidase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase number of possible subsites: three Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Ala-4-nitroanilide + H2O
-
Rattus norvegicus acetyl-Ala + 4-nitroaniline
-
ir
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro + H2O
-
Rattus norvegicus benzyloxycarbonyl-Pro-Ala-Ala-Ala + Pro
-
ir
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro-NH2 + H2O
-
Rattus norvegicus benzyloxycarbonyl-Pro-Ala-Ala-Ala + Pro-NH2
-
ir
additional information influence of Pro in position P1 to P3 on rate of peptide hydrolysis, P3 i.e. 3rd amino acid in N-terminal direction relative to point of cleavage, greatest increase in activity after substrate elongation to tetrapeptide Rattus norvegicus ?
-
?
Proteins + H2O rather broad specificity of aminopeptidase activity Rattus norvegicus ?
-
?
succinyl-Ala-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Ala + 4-nitroaniline
-
ir
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Ala + 4-nitroaniline
-
ir
succinyl-Ala-Ala-Ala-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Ala-Ala + 4-nitroaniline
-
ir
succinyl-Ala-Ala-Ala-Ala-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Ala-Ala-Ala + 4-nitroaniline
-
ir
succinyl-Ala-Ala-Pro-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Pro + 4-nitroaniline
-
ir
succinyl-Ala-Pro-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Ala-Pro-Ala + 4-nitroaniline
-
ir
succinyl-Pro-Ala-Ala-4-nitroanilide + H2O
-
Rattus norvegicus succinyl-Pro-Ala-Ala + 4-nitroaniline
-
ir

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.004
-
succinyl-Ala-Ala-Pro-4-nitroanilide
-
Rattus norvegicus
0.07
-
succinyl-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
0.15
-
succinyl-Pro-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
0.3
-
succinyl-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
0.8
-
succinyl-Ala-Ala-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
0.9
-
succinyl-Ala-Ala-Ala-Ala-4-nitroanilide
-
Rattus norvegicus
5.3
-
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro
-
Rattus norvegicus
7.7
-
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro-NH2
-
Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Rattus norvegicus