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Tritium exchange reactions catalyzed by 2-oxo-4-hydroxyglutarate aldolase from Escherichia coli K-12.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Grady, Sharon R. Dekker, Eugene E. |
| Copyright Year | 1979 |
| 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 in equilibrium 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. |
| Starting Page | 1 |
| Ending Page | 72 |
| Page Count | 72 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://deepblue.lib.umich.edu/bitstream/handle/2027.42/23566/0000526.pdf;jsessionid=4C286BA96A43816170E029751C515D36?sequence=1 |
| PubMed reference number | 375986v1 |
| Volume Number | 568 |
| Issue Number | 1 |
| Journal | Biochimica et biophysica acta |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | 2-ketobutyrate 4-Hydroxy-2-oxoglutarate aldolase Acetaldehyde Analog Betaine-aldehyde dehydrogenase Fructosediphosphate Aldolase Glyoxylates Hydrogen Peroxide 30 MG/ML Topical Solution Lyase Methylmethacrylate Pyruvates Tritium carbene |
| Content Type | Text |
| Resource Type | Article |
