Tritium exchange reactions catalyzed by 2-oxo-4-hydroxyglutarate aldolase from Escherichia coli K-12
dc.contributor.author | Grady, Sharon R. | en_US |
dc.contributor.author | Dekker, Eugene E. | en_US |
dc.date.accessioned | 2006-04-07T17:34:52Z | |
dc.date.available | 2006-04-07T17:34:52Z | |
dc.date.issued | 1979-05-10 | en_US |
dc.identifier.citation | Grady, Sharon R., Dekker, Eugene E. (1979/05/10)."Tritium exchange reactions catalyzed by 2-oxo-4-hydroxyglutarate aldolase from Escherichia coli K-12." Biochimica et Biophysica Acta (BBA) - Enzymology 568(1): 234-242. <http://hdl.handle.net/2027.42/23566> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GH-47T8XV8-2S/2/54d79ada27c3c077ab5eba6cc6eb2d15 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23566 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=375986&dopt=citation | en_US |
dc.description.abstract | Tritiated water and tritiated substrates have been used to study exchange reactions catalyzed by Escherichia coli 2-oxo-4-hydroxyglutarate aldolase (4-hydroxy-2-oxoglutarate glyoxylate-lyase, EC 4.1.3.16, 2-oxo-4-hydroxyglutarate [right harpoon over left] pyruvate + glyoxylate). With pyruvate, the enzyme catalyzes a rapid first-order exchange of all three methyl hydrogens in the absence of added acceptor aldehyde (i.e. glyoxylate). This reaction is not rate limiting for aldol condensation or cleavage; quite different pH-activity profiles for the exchange reaction versus aldol cleavage and also comparative effects that pH changes have on Km and V values for the two processes favor this conclusion. The exchange reaction with 2-oxobutyrate, a substrate analog, is stereoselective; one methylene hydrogen is removed at a 6-fold faster rate than the other but eventually both are exchanged. No tritium exchange occurs with glyoxylate. | en_US |
dc.format.extent | 615722 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Tritium exchange reactions catalyzed by 2-oxo-4-hydroxyglutarate aldolase from Escherichia coli K-12 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 375986 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23566/1/0000526.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2744(79)90290-0 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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