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3.4.14.5: dipeptidyl-peptidase IV

This is an abbreviated version!
For detailed information about dipeptidyl-peptidase IV, go to the full flat file.

Word Map on EC 3.4.14.5

Reaction

release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline =

Synonyms

(GLP1)-degrading enzyme, ACT3, ADA binding protein, ADA-binding protein, ADABP, adenosine deaminase binding protein, Adenosine deaminase complexing protein, adenosine deaminase-binding protein, amino acyl-prolyl dipeptidyl aminopeptidase, aminopeptidase, glycylproline, Bile canaliculus domain-specific membrane glycoprotein, CD26, CD26 peptidase, CD26/dipeptidyl peptidase, CD26/DP IV, DAP IV, DapB, dapUm, dipeptidyl aminopeptidase IV, dipeptidyl dipeptidase IV, dipeptidyl peptidase 4, dipeptidyl peptidase 8, dipeptidyl peptidase 9, dipeptidyl peptidase IV, dipeptidyl peptidase-4, dipeptidyl peptidase-IV, dipeptidyl-aminopeptidase IV, dipeptidyl-peptidase 4, dipeptidyl-peptidase IV (CD26), dipeptidyl-peptide hydrolase, dipeptidylpeptidase 4a, dipeptidylpeptidase 4b, dipeptidylpeptidase IV, dipeptidylpeptidase IV/CD26, dipeptidylpeptidase-IV, DP IV, DP-IV, DPIV, DPP, DPP IV, DPP IV/CD26, DPP-4, DPP-IV, DPP4, DPP8, DPP9, DPPIV, DppIVA, DppIVB, glucagon-like peptide 1-degrading enzyme, Gly-Pro-naphthylamidase, glycoprotein GP110, glycylproline aminopeptidase, glycylproline-dipeptidyl-aminopeptidase, glycylprolyl aminopeptidase, glycylprolyl dipeptidylaminopeptidase, GP110 glycoprotein, h-DPPIV, hDPPIV, leukocyte antigen CD26, lymphocyte, antigen CD26, More, omega DPPIV, omega enzyme, omega gene product, Pep X, peptidase, dipeptidyl, IV, PepX, postproline dipeptidyl aminopeptidase IV, prolyl-dipeptidyl-aminopeptidase, sipeptidyl peptidase IV, T cell triggering molecule Tp103, T-cell activation antigen CD26, THAM, Thymocyte-activating molecule, TP103, type IV dipeptidyl aminopeptidase, WC10, X-PDAP, X-prolyl dipeptidyl aminopeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro-dipeptidyl-aminopeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases
                3.4.14.5 dipeptidyl-peptidase IV

Crystallization

Crystallization on EC 3.4.14.5 - dipeptidyl-peptidase IV

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant soluble enzyme ectodomain, vapour diffusion method, with 20-25% PEG 3350, 0.2 M MgCl2, Tris, pH 8.5, 15% glycerol, flash-frozen crystals for X-ray diffraction structure determination and analysis at 2.1 A resolution, also preparation and study of a mercury derivative
20 mg/ml purified soluble extracellular domain apoprotein, glycosidase endo-F treated, in 25 mM Tris, pH 7.5, 100 mM NaCl, 2 mM Tris(2-carboxyethyl)phosphine hydrochloride, i.e. TCEP, 5% glycerol, modified microbatch method, hanging drop vapour diffusion method, from 25% PEG 3350, 200 mM MgCl2, 100 mM HEPES, pH 7.5, complexing with inhibitor 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano(S)-pyrrolidine, several days, X-ray diffraction structure determination and analysis at 1.9 A resolution, in cryoprotectant solution containing 25% PEG 3350, 20% 1,6-hexanediol, at 100 K
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20 mg/ml recombinant soluble enzyme, sitting drop vapour diffusion method, 293 K, from 180 mM Gly-NaOh, pH 9.5, with 180 mM sodium acetate and 18% PEG 4000, crystal grow 2 weeks after seeding, X-ray diffraction structure determination and analysis at 2.6 A resolution
40 mg/ml extracellular enzyme region complexed with inhibitor valine-pyrrolidine in 20 mM Tris, pH 8.0, ans 25 mM NaCl, sitting drop vapour diffusion method, mixed with equal volume of reservoir solution containing 0.3 M sodium acetate, 17-18% w/v PEG 4000, 0.1 M Tris, pH 8.0, 2-3 days, X-ray diffraction structure determination and analysis at 2.5 A resolution
crystal structure of apo hDPPIV at 1.9 A resolution, crystal structure of hDPPIV-diprotin B (Val-Pro-Leu) complex at 2.1 A resolution
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crystal structure of apo hDPPIV at 1.9 A resolution. Crystal structure of hDPPIV-diprotin B complex at 2.1 A resolution
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crystal structure of human CD26/dipeptidyl-peptidase IV in complex with bovine adenosine deaminase reveals a highly amphiphilic interface, structure determined at 3.0 A resolution
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°
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dipeptidyl peptidase IV complex with diprotin A, a slowly hydrolyzed substrate at 2.2 A, space group: P2(1)2(1)2(1), cell dimensions: a = 118.02 A, b * 126.06 A, c = 136.67 A
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hanging drop vapor diffusion method, crystallization of apoenzyme, mutant enzyme Y547F and DPP-IV in complex with diisopropyl fluorophosphate. X-ray crystal structurte analysis of the Y547 mutant reveals no overal changes compared with wild-type apoDPP-IV, except the ablation of the hydroxyl group of Tyr547 and a water molecule positioned in close proximity to Tyr547
in complex with inhibitor (3R)-4-[(3R)-3-amino-4-(2,4,5-trifluorophenyl)butanoyl]-3-[(2-methylpropan-2-yl)oxymethyl]piperazin-2-one. The binding of the trifluorophenyl moiety in the S1 pocket and the piperazine-2-one moiety have hydrophobic interactions with Phe357 in the S2 extensive subsite, and the multiple hydrogen bonds made by the (R)-beta-amine group in the S2 pocket and the contacts made by the (R)-tert-butyl group with Arg125 contribute to the high potency of the inhibitor
in complex with inhibitor N-[(3R)-3-amino-4-(2,4,5-trifluorophenyl)butyl]-6-(trifluoromethyl)-3,4-dihydropyrrolo[1,2-a]pyrazine-2(1H)-carboxamide, to 3.2 A resolution
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molecular docking simulaion for compounds ethyl-2-(4-(((S)-1-((S)-2-amino-(4-fluorophenyl)propanoyl)pyrrolidine-2-carboxamido)-methyl)phenoxy)acetate and ethyl-2-(4-(((S)-1-((S)-2-amino-3-(2-fluorophenyl)propanoyl)pyrrolidine-2-carboxamido)-methyl)phenoxy)acetate
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
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recombinant enzyme forms dimers in crystals
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X-ray diffraction strcuture determination at 2.6 A resolution
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purified recombinant enzyme, hanging drop method using 5-10% PEG 4000, pH 5.2, 18°C, preparation of heavy atom derivatives, X-ray diffraction structure determination and analysis at 2.2 A resolution
hanging-drop vapour-diffusion technique in 40% 2-methyl-2,4-pentanediol and 100 mM Tris/HCl pH 8.0. Diffraction data to 2.7 A resolution are collected using synchrotron radiation. The crystals belong to space group P2(1), with unit-cell parameters a = 117.0 A, b = 112.9 A, c = 310.0 A, beta = 95°. There are ten molecules per asymmetric unit, indicating a solvent content of 50%
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structures of free form and in complexes with dipeptides Lys-Pro or Ile-Pro as well as with a non-peptidyl inhibitor at 1.90 to 2.47 A resolution. Acyl-enzyme intermediates are observed for the dipeptide complexes, whereas tetrahedral intermediates are reported for the oligopeptide complexes of mammalian DPP IVs
to 1.9 A resolution, in complex with peptide in complex with the tripeptide Lys-Pro-Tyr
vapor diffusion method, 2.8 A resolution
20 mg/ml purified enzyme, sitting drop vapour diffusion method, room temperature, several days, from 20-22% PEG 2000, 0.1 ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, covering of the drops with perfluoropolyether oil, humidity control during harvest of crystals, multiple wavelength anomalous dispersion using a mercury derivative and subsequent noncrystallographic symmetry averaging, structure determination and analysis, modeling
DPIV complexes with a t-butyl-Gly-Pro-Ile tripeptide, Pro-boroPro, tert-butyl-Gly-L-Pro-L-Ile, 7-benzyl-1,3-dimethyl-8-piperazin-1-yl-3,7-dihydro-purine-2,6-dione and 4-(2-aminoethyl)-benzene sulfonyl fluoride
enzyme forms tetramers in crystals, which may depend on native glycosylation
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