Cd2+ activation of -threonine dehydrogenase from Escherichia coli K-12
dc.contributor.author | Craig, Paul A. | en_US |
dc.contributor.author | Dekker, Eugene E. | en_US |
dc.date.accessioned | 2006-04-07T20:08:22Z | |
dc.date.available | 2006-04-07T20:08:22Z | |
dc.date.issued | 1988-11-23 | en_US |
dc.identifier.citation | Craig, Paul A., Dekker, Eugene E. (1988/11/23)."Cd2+ activation of -threonine dehydrogenase from Escherichia coli K-12." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 957(2): 222-229. <http://hdl.handle.net/2027.42/27060> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T21-488GG7X-9/2/221a80a95467c98fc4d3191cb03ed1c7 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/27060 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3056527&dopt=citation | en_US |
dc.description.abstract | Homogeneous preparations of -threonine dehydrogenase (-threonine: NAD+ oxidoreductase, EC 1.1.1.103) from Escherichia coli K-12, after having been dialyzed against buffers containing Chelex-100 resin, have a basal level of activity of 10-20 units/mg. Added Cd2+ stimulates dehydrogenase activity approx. 10-fold; this activation is concentration-dependent and is saturable with an activation Kd = 0.9 [mu]M. Full activation by Cd2+ is obtained in the absence of added thiols. The pH-activity profile of the Cd2+-activated enzyme conforms to a theoretical curve for one-proton ionization with a pKa = 7.85. Mn2+, the only other activating metal ion, competes with Cd2+ for the same binding site. Km values for -threonine and NAD+ as well as the Vmax for `demetallized', Cd2+-activated, and Mn2+-activated threonine dehydrogenase were determined and compared. | en_US |
dc.format.extent | 1060276 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 | Cd2+ activation of -threonine dehydrogenase 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, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI, U.S.A. | en_US |
dc.identifier.pmid | 3056527 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/27060/1/0000050.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0167-4838(88)90276-2 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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