Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.14.5 extracted from

  • Hiramatsu, H.; Kyono, K.; Higashiyama, Y.; Fukushima, C.; Shima, H.; Sugiyama, S.; Inaka, K.; Yamamoto, A.; Shimizu, R.
    The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold (2003), Biochem. Biophys. Res. Commun., 302, 849-854.
    View publication on PubMed

Application

Application Comment Organism
pharmacology target for development of selective inhibitors for control of the enzyme's biological function Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction strcuture determination at 2.6 A resolution Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens enzyme is implicated in several diseases ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline serine protease Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is implicated in several diseases Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More enzyme possesses a unique eight-bladed beta-propeller fold Homo sapiens

Synonyms

Synonyms Comment Organism
dipeptidyl peptidase IV
-
Homo sapiens
DPPIV
-
Homo sapiens
More enzyme belongs to the prolyl oligopeptidase POP family Homo sapiens