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Literature summary for 3.4.14.5 extracted from

  • Cohen, M.; Fruitier-Arnaudin, I.; Piot, J.M.
    Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV. Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV (2004), Biochimie, 86, 31-37.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Diprotin A
-
Rattus norvegicus
hemorphin-4 peptide 12% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence YPWT, competitive Rattus norvegicus
hemorphin-5 peptide 18% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence YPWTQ, competitive Rattus norvegicus
hemorphin-7 peptide 30% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence YPWTQRF, selective and competitive Rattus norvegicus
LVV-hemorphin-7 peptide 9% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence LVVYPWTQRF, the additional leucine residue reduces the inhibitory potential Rattus norvegicus
additional information inhibitory mechanism, the N-terminus sequence of hemorphins influence the interaction between hemorphins and the enzyme Rattus norvegicus
VV-hemorphin-5 peptide 10% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence VVYPWTQ Rattus norvegicus
VV-hemorphin-6 peptide 15% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence VVYPWTQR Rattus norvegicus
VV-hemorphin-7 peptide 27% inhibition at 0.03 mM, endogenous blood-derived peptide belonging to the family of atypical opioidic peptides released from sequentially hydrolyzed hemoglobin, amino acid sequence VVYPWTQRF Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0387
-
hemorphin-7 pH 8.0, 37°C, microsomes Rattus norvegicus
0.38
-
Gly-Pro-4-nitroanilide pH 8.0, 37°C, microsomes Rattus norvegicus
6.4
-
hemorphin-5 pH 8.0, 37°C, microsomes Rattus norvegicus
13.5
-
hemorphin-4 pH 8.0, 37°C, microsomes Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Rattus norvegicus 16020
-
microsome
-
Rattus norvegicus
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus hemorphins may represent endogenous regulators of the enzyme activity ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
male Wistar rats
-

Purification (Commentary)

Purification (Comment) Organism
partial, preparation of microsomal fraction Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Pro-4-nitroanilide + H2O
-
Rattus norvegicus Gly-Pro + 4-nitroaniline
-
?
hemorphin-4 + H2O
-
Rattus norvegicus YP + WT
-
?
hemorphin-5 + H2O
-
Rattus norvegicus YP + WTQ
-
?
hemorphin-7 + H2O
-
Rattus norvegicus YP + WTQRF
-
?
additional information LVV-hemorphin-7 and LVV-hemorphin-6 are no substrates for the enzyme Rattus norvegicus ?
-
?
additional information hemorphins may represent endogenous regulators of the enzyme activity Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
dipeptidyl peptidase IV
-
Rattus norvegicus
DPPIV
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3
-
hemorphin-7 pH 8.0, 37°C, microsomes Rattus norvegicus
52.3
-
Gly-Pro-4-nitroanilide pH 8.0, 37°C, microsomes Rattus norvegicus
1770
-
hemorphin-4 pH 8.0, 37°C, microsomes Rattus norvegicus
1774
-
hemorphin-4 pH 8.0, 37°C, microsomes Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Rattus norvegicus
0.029
-
VV-hemorphin-7 peptide pH 8.0, 37°C, microsomes Rattus norvegicus
0.033
-
hemorphin-7 peptide pH 8.0, 37°C, microsomes Rattus norvegicus