Literature summary for 3.4.14.5 extracted from

Aertgeerts, K.; Ye, S.; Tennant, M.G.; Kraus, M.L.; Rogers, J.; Sang, B.C.; Skene, R.J.; Webb, D.R.; Prasad, G.S.
Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation (2004), Protein Sci., 13, 412-421.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of soluble His-tagged enzyme wild-type and a selenomethionine forms, which comprise extracellular domain amino acid residues 39-766 and are secreted to the medium, in Trichoplusia ni Hi5 insect cells via baculovirus infection	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the free form of DPPIV and of the enzyme in complex with the first 10 residues of the physiological substrate neuropeptide Y (tNPY). The structure of the enzyme/tNPY complex suggests that bioactive peptides utilize the side opening unique to DPPIV to access the active site. Space group of wild-type enzyme and enzyme/tNPY complex is P2(1). The cell dimensions for wild-type enzyme are a = 121.8 A, b = 124,1 A, c = 1445 A, beta = 114.7°. The cell dimensions for the enzyme /tNPY complex are a = b = 122.5 A, c = 145.3 A, beta = 114.9°	Homo sapiens
purified recombinant enzyme extracellular domain, wild-type or selenomethionine-form, both free, and the wild-type also complexed with the decapeptide YPSKPDNPGE, corresponding to the first 10 amino acids of neuropeptide Y, 4°C, nanovolume crystallization, over reservoir solution containing 20% PEG monomethyl ester 2000, 100 mM bicine, pH 8.0-8.5, 5 days, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, at 100 K using 25% v/v ethylene glycol as a cryoprotectant	Homo sapiens

Crystallization (Comment)

Organism

crystal structure of the free form of DPPIV and of the enzyme in complex with the first 10 residues of the physiological substrate neuropeptide Y (tNPY). The structure of the enzyme/tNPY complex suggests that bioactive peptides utilize the side opening unique to DPPIV to access the active site. Space group of wild-type enzyme and enzyme/tNPY complex is P2(1). The cell dimensions for wild-type enzyme are a = 121.8 A, b = 124,1 A, c = 1445 A, beta = 114.7°. The cell dimensions for the enzyme /tNPY complex are a = b = 122.5 A, c = 145.3 A, beta = 114.9°

Homo sapiens

purified recombinant enzyme extracellular domain, wild-type or selenomethionine-form, both free, and the wild-type also complexed with the decapeptide YPSKPDNPGE, corresponding to the first 10 amino acids of neuropeptide Y, 4°C, nanovolume crystallization, over reservoir solution containing 20% PEG monomethyl ester 2000, 100 mM bicine, pH 8.0-8.5, 5 days, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, at 100 K using 25% v/v ethylene glycol as a cryoprotectant

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	N-glycosylation sites are N85, N92, N150, N219, N229, N281, N321, N520, N685, glycosylation is not important for catalytic activity, homodimer formation and adenosine deaminase binding	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant soluble His-tagged wild-type and selenomethionine enzymes from insect cell culture supernatant to homogeneity	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	prefers Pro or Ala at position P1, substrate recognition involves the negatively charged active site residues E205 and E206, reaction mechanism, active site structure and substrate binding	Homo sapiens	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
spleen	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
Ala-Pro-7-amido-4-methylcoumarin + H2O	-	Homo sapiens	Ala-Pro + 7-amino-4-methylcoumarin	-	?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O	-	Homo sapiens	Ala-Pro + 7-amino-4-trifluoromethylcoumarin	-	?
additional information	substrate specificity, enzyme binds adenosine deaminase	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimer, crystal structure, not affected by glycosylation state, domain structure, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ADABP	-	Homo sapiens
adenosine deaminase binding protein	-	Homo sapiens
CD26	-	Homo sapiens
dipeptidyl peptidase IV	-	Homo sapiens
DPPIV	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Homo sapiens