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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03959naa a2200409 4500 | |
| 001 | oai:DiVA.org:kth-9749 | |
| 003 | SwePub | |
| 008 | 081205s2008 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-97492 URI |
| 024 | 7 | a https://doi.org/10.1021/bi800971v2 DOI |
| 040 | a (SwePub)kth | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Kim, Jungwooku Albert Einstein Coll Med4 aut |
| 245 | 1 0 | a Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase |
| 264 | c 2008-08-15 | |
| 264 | 1 | b American Chemical Society (ACS),c 2008 |
| 338 | a print2 rdacarrier | |
| 500 | a QC 20100714 | |
| 520 | a The bacterial phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the hydrolysis of organophosphate esters at rates close to the diffusion limit. X-ray diffraction studies have shown that a binuclear metal center is positioned in the active site of PTE and that this complex is responsible for the activation of the nucleophilic water from solvent. In this paper, the three-dimensional structure of PTE was determined in the presence of the hydrolysis product, diethyl phosphate (DEP), and a product analogue, cacodylate. In the structure of the PTE−diethyl phosphate complex, the DEP product is found symmetrically bridging the two divalent cations. The DEP displaces the hydroxide from solvent that normally bridges the two divalent cations in structures determined in the presence or absence of substrate analogues. One of the phosphoryl oxygen atoms in the PTE−DEP complex is 2.0 Å from the α-metal ion, while the other oxygen is 2.2 Å from the β-metal ion. The two metal ions are separated by a distance of 4.0 Å. A similar structure is observed in the presence of cacodylate. Analogous complexes have previously been observed for the product complexes of isoaspartyl dipeptidase, d-aminoacylase, and dihydroorotase from the amidohydrolase superfamily of enzymes. The experimentally determined structure of the PTE−diethyl phosphate product complex is inconsistent with a recent proposal based upon quantum mechanical/molecular mechanical simulations which postulated the formation of an asymmetrical product complex bound exclusively to the β-metal ion with a metal−metal separation of 5.3 Å. This structure is also inconsistent with a chemical mechanism for substrate hydrolysis that utilizes the bridging hydroxide as a base to abstract a proton from a water molecule loosely associated with the α-metal ion. Density functional theory (DFT) calculations support a reaction mechanism that utilizes the bridging hydroxide as the direct nucleophile in the hydrolysis of organophosphate esters by PTE. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a BACTERIAL PHOSPHOTRIESTERASE; PSEUDOMONAS-DIMINUTA; ISOASPARTYL DIPEPTIDASE; REACTION-MECHANISM; ESCHERICHIA-COLI; D-AMINOACYLASE; HYDROLYSIS; DENSITY; ENZYME; ENERGY | |
| 653 | a Biochemistry | |
| 653 | a Biokemi | |
| 700 | 1 | a Tsai, Ping-Chuanu Texas A&M Univ, Dept Chem4 aut |
| 700 | 1 | a Chen, Shiluu KTH,Teoretisk kemi4 aut0 (Swepub:kth)u1jm35sc |
| 700 | 1 | a Himo, Fahmiu KTH,Teoretisk kemi4 aut0 (Swepub:kth)u1hl0yc6 |
| 700 | 1 | a Almo, Steven C.u Albert Einstein Coll Med4 aut |
| 700 | 1 | a Raushel, Frank M.u Texas A&M Univ, Dept Chem4 aut |
| 710 | 2 | a Albert Einstein Coll Medb Texas A&M Univ, Dept Chem4 org |
| 773 | 0 | t Biochemistryd : American Chemical Society (ACS)g 47:36, s. 9497-9504q 47:36<9497-9504x 0006-2960x 1520-4995 |
| 856 | 4 | u https://europepmc.org/articles/pmc2725523?pdf=render |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-9749 |
| 856 | 4 8 | u https://doi.org/10.1021/bi800971v |
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