Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The derivatization of prostaglandins of the A series with 1:1 mixtures of bis-(trimethylsilyl)trifluoroacetamide and nitrogen-containing non-aromatic heterocyclics such as piperidine, pyrrolidine, morpholine and hexamethylenimine (1--4 h at 60--70 degrees C) gives new types of derivatives, designated as 11-heterocycle, 9-enol PGA (TMS)3. These derivatives show very simplified and characteristic mass spectral patterns strikingly dominated by a common [M-173]+ fragment ion and easily detectable by selected ion monitoring. This feature allows the concurrent analytical detection of both prostaglandin A's and 19-hydroxy prostaglandin A's in biological samples. In this case 2 ml samples of human semen were extracted by direct ultrafiltration on a Pellicon membrane with a nominal molecular weight limit of 1000. The prostaglandins in the approximately or equal to 1.6 ml of ultrafiltrate thus obtained were recovered in ethyl acetate, derivatized as indicated above and detected by monitoring of the corresponding [M-173]+ ions.
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PMID:New derivatives of prostaglandin A1 and specific detection of prostaglandin A's and 190hydroxylated prostaglandin A's in human semen. 70 54

The atomic resolution structure of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate shows that this transition state analogue is bound in two conformations. Also for the side chain of the catalytic glutamate, Glu(167), two conformations are observed. In both conformations, a very short hydrogen bond exists between the carboxylate group of the ligand and the catalytic glutamate. The distance between O11 of PGA and Oepsilon2 of Glu(167) is 2.61 and 2.55 A for the major and minor conformations, respectively. In either conformation, Oepsilon1 of Glu(167) is hydrogen-bonded to a water network connecting the side chain with bulk solvent. This network also occurs in two mutually exclusive arrangements. Despite the structural disorder in the active site, the C termini of the beta strands that construct the active site display the least anisotropy compared with the rest of the protein. The loops following these beta strands display various degrees of anisotropy, with the tip of the dimer interface loop 3 having very low anisotropy and the C-terminal region of the active site loop 6 having the highest anisotropy. The pyrrolidine ring of Pro(168) at the N-terminal region of loop 6 is in a strained planar conformation to facilitate loop opening and product release.
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PMID:Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution. 1252 13