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Literature summary for 3.4.14.5 extracted from

  • Chien, C.; Tsai, C.; Lin, C.; Chou, C.; Chen, X.
    Identification of hydrophobic residues critical for DPP-IV dimerization (2006), Biochemistry, 45, 7006-7012.
    View publication on PubMed
Search for more literature for 3.4.14.5

Protein Variants

Protein Variants Comment Organism
F713A mutation disrupts dimeric DPP-IV into monomers. kcat/Km for Gly-Pro-p-nitroaniline is 27fold lower wild-type value Homo sapiens
F730A mutant enzyme is a mixture of monomers and dimers. With the dimeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1.9fold lower than wild-type value. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 241fold lower than wild-type value Homo sapiens
V724A mutant enzyme remains largely dimeric. With the dimeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1.8fold lower than wild-type value. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 138fold lower than wild-type value Homo sapiens
W734A mutation disrupts dimeric DPP-IV into monomers with a small fraction of dimers. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 322fold lower than wild-type value Homo sapiens
Y735A mutation disrupts dimeric DPP-IV into monomers. With the monomeric mutant enzyme the kcat/Km for Gly-Pro-p-nitroaniline is 1612fold lower than wild-type value Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme F713A Homo sapiens
0.054
-
 Gly-Pro-p-nitroanilide monomeric mutant enzymeF730A Homo sapiens
0.056
-
 Gly-Pro-p-nitroanilide dimeric mutant enzyme F730A Homo sapiens
0.076
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme V724A Homo sapiens
0.088
-
 Gly-Pro-p-nitroanilide dimeric mutant enzyme C724A Homo sapiens
0.089
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme Y735A Homo sapiens
0.09
-
 Gly-Pro-p-nitroanilide dimeric rDPP-IV Homo sapiens
0.09
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme W734A Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens homodimeric DPP-IV interacts extracellularly with adenosine deaminase, and this interaction is critical for adenosine signaling and T-cell proliferation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P27487 recombinant
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Pro-p-nitroanilide + H2O
-
 Homo sapiens Gly-Pro + p-nitroaniline
-
 ?
additional information homodimeric DPP-IV interacts extracellularly with adenosine deaminase, and this interaction is critical for adenosine signaling and T-cell proliferation Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
dimer hydrophobic residues F713, W734, and Y735 are essential for DPP-IV dimerization. Monomeric DPP-IV has residual activity left, ranging from 1/30 to 1/1600 of the dimeric forms. The affinity of these DPP-IV monomers for adenosine deaminase is not significantly altered, compared to that of dimeric DPP-IV Homo sapiens

Synonyms

Synonyms Comment Organism
DPP-IV
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme Y735A Homo sapiens
0.2
-
 Gly-Pro-p-nitroanilide monomeric mutant enzymeF730A Homo sapiens
0.3
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme W734A Homo sapiens
0.5
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme V724A Homo sapiens
1.8
-
 Gly-Pro-p-nitroanilide monomeric mutant enzyme F713A Homo sapiens
2 8 Gly-Pro-p-nitroanilide dimeric mutant enzyme F730A Homo sapiens
48
-
 Gly-Pro-p-nitroanilide dimeric mutant enzyme C724A Homo sapiens
87
-
 Gly-Pro-p-nitroanilide dimeric rDPP-IV Homo sapiens