Enzymes
| UniProtKB help_outline | 1 proteins |
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Reaction participants Show >> << Hide
- Name help_outline A Identifier CHEBI:13193 Charge Formula R SMILEShelp_outline * 2D coordinates Mol file for the small molecule Search links Involved in 2,870 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-proline Identifier CHEBI:57726 Charge 0 Formula C5H9NO2 InChIKeyhelp_outline ONIBWKKTOPOVIA-SCSAIBSYSA-N SMILEShelp_outline [O-]C(=O)[C@H]1CCC[NH2+]1 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-pyrroline-2-carboxylate Identifier CHEBI:39785 Charge 0 Formula C5H7NO2 InChIKeyhelp_outline RHTAIKJZSXNELN-UHFFFAOYSA-N SMILEShelp_outline [O-]C(=O)C1=[NH+]CCC1 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AH2 Identifier CHEBI:17499 Charge 0 Formula RH2 SMILEShelp_outline *([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 2,799 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:27306 | RHEA:27307 | RHEA:27308 | RHEA:27309 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane.
Tani Y., Tanaka K., Yabutani T., Mishima Y., Sakuraba H., Ohshima T., Motonaka J.
A novel biosensor for determination of d-amino acids (DAAs) in biological samples by using an electrode based on immobilization of a thermostable d-Proline dehydrogenase (d-Pro DH) within an agar gel membrane was developed. The electrode was simply prepared by spin-coating the agar solution with t ... >> More
A novel biosensor for determination of d-amino acids (DAAs) in biological samples by using an electrode based on immobilization of a thermostable d-Proline dehydrogenase (d-Pro DH) within an agar gel membrane was developed. The electrode was simply prepared by spin-coating the agar solution with the d-Pro DH on a glassy carbon (GC) electrode. An electrocatalytic oxidation current of 2,6-dichloroindophenol (DCIP) was observed at -100mV vs. Ag/AgCl with the addition of 5 and 20mmolL(-1)d-proline. The current response and its relative standard deviation were 0.15muA and 7.6% (n=3), respectively, when it was measured in a pH 8.0 phosphate buffer solution containing 10mmolL(-1)d-proline and 0.5mmolL(-1) DCIP at 50 degrees C. The current response of d-proline increased with increase of the temperature of the sample solution up to 70 degrees C. The electrocatalytic response at the d-Pro DH/agar immobilized electrode subsequently maintained for 80 days. Finally, the d-Pro DH/agar immobilized electrode was applied to determination of DAAs in a human urine sample. The determined value of DAAs in the human urine and its R.S.D. were 1.39+/-0.12mmolL(-1) and 8.9% (n=3), respectively. << Less
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Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase.
Satomura T., Kawakami R., Sakuraba H., Ohshima T.
The activity of dye-linked d-proline dehydrogenase was found in the crude extract of a hyperthermophilic archaeon, Pyrobaculum islandicum JCM 9189. The dye-linked d-proline dehydrogenase was a membrane associated enzyme and was solubilized from the membrane fractions by treatment with Tween 20. Th ... >> More
The activity of dye-linked d-proline dehydrogenase was found in the crude extract of a hyperthermophilic archaeon, Pyrobaculum islandicum JCM 9189. The dye-linked d-proline dehydrogenase was a membrane associated enzyme and was solubilized from the membrane fractions by treatment with Tween 20. The solubilized enzyme was purified 34-fold in the presence of 0.1% Tween 20 by four sequential chromatographies. The enzyme has a molecular mass of about 145 kDa and consisted of homotetrameric subunits with a molecular mass of about 42 kDa. The N-terminal amino acid sequence of the subunit was MKVAIVGGGIIGLFTAYHLRQQGADVVI. The enzyme retained its full activity both after incubation at 80 degrees C for 10 min and after incubation in the range of pH 4.0-10.0 at 50 degrees C for 10 min. The enzyme-catalyzed dehydrogenation of several d-amino acids was carried out using 2,6-dichloroindophenol as an electron acceptor, and d-proline was the most preferred substrate among the d-amino acids. The Michaelis constants for d-proline and 2,6-dichloroindophenol were determined to be 4.2 and 0.14 mm, respectively. Delta(1)-Pyrroline-2-carboxylate was identified as the reaction product from d-proline by thin layer chromatography. The prosthetic group of the enzyme was identified to be FAD by high-performance liquid chromatography. The gene encoding the enzyme was cloned and expressed in Escherichia coli. The nucleotide sequence of the dye-linked d-proline dehydrogenase gene was determined and encoded a peptide of 363 amino acids with a calculated molecular weight of 40,341. The amino acid sequence of the Pb. islandicum enzyme showed the highest similarity (38%) with that of the probable oxidoreductase in Sulfolobus solfataricus, but low similarity with those of d-alanine dehydrogenases from the mesophiles so far reported. This shows that the membrane-bound d-proline dehydrogenase from Pb. islandicum is a novel FAD-dependent amino acid dehydrogenase. << Less