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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
1987-9-17
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pubmed:abstractText |
5-Oxoprolinase catalyzes a reaction in which the cleavage of ATP to ADP and Pi and the decyclization of 5-oxoproline to form glutamate are coupled. When the reaction catalyzed by 5-oxoprolinase of Pseudomonas putida was carried out to 90% completion in H2(18)O, the residual 5-oxoproline was found to contain 18O in the amide carbonyl oxygen atom. Such isotopic incorporation was not observed in similar studies with a subunit of the enzyme which catalyzes 5-oxoproline-dependent ATPase and formation of a phosphorylated 5-oxoproline intermediate (Seddon, A.P., and Meister, A. (1986) J. Biol. Chem. 261, 11538-11543). When the complete reaction was carried out in H2(18)O, the products glutamate (gamma-carboxyl) and inorganic phosphate were mono- and di-labeled with 18O. Studies with 5-[18O]oxo-L-proline confirmed such replacement of the oxygen atoms of the gamma-carboxyl group of glutamate and the carbonyl oxygen of 5-oxoproline. Oxygen was not transferred from 5-oxoproline to inorganic phosphate. Studies with analogs of 5-oxoproline showed that di-labeling of inorganic phosphate occurred only when ATP hydrolysis was coupled or partially coupled with the decyclization of the substrate. Studies with 5-oxoprolinase from rat kidney gave similar results. These observations are in accord with the view that the reaction involves enzyme-bound phosphorylated intermediates and provide evidence for a phosphorylated tetrahedral intermediate, whose formation is required for coupling.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Carboxyglutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen Isotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pyroglutamate Hydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidonecarboxylic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11020-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3611103-1-Carboxyglutamic Acid,
pubmed-meshheading:3611103-Adenosine Diphosphate,
pubmed-meshheading:3611103-Adenosine Triphosphate,
pubmed-meshheading:3611103-Amidohydrolases,
pubmed-meshheading:3611103-Animals,
pubmed-meshheading:3611103-Kidney,
pubmed-meshheading:3611103-Oxygen Isotopes,
pubmed-meshheading:3611103-Phosphates,
pubmed-meshheading:3611103-Phosphoproteins,
pubmed-meshheading:3611103-Phosphorylation,
pubmed-meshheading:3611103-Pseudomonas,
pubmed-meshheading:3611103-Pyroglutamate Hydrolase,
pubmed-meshheading:3611103-Pyrrolidonecarboxylic Acid,
pubmed-meshheading:3611103-Rats
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pubmed:year |
1987
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pubmed:articleTitle |
18O studies on the 5-oxoprolinase reaction. Evidence for a phosphorylated tetrahedral intermediate.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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