Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB)--implications for carbapenem biosynthesis.
Carboxymethylproline synthase was shown to condense L-glutamate semialdehyde with malonyl-coenzyme A to produce (2S,5S)-carboxymethylproline, while incubation of D-glutamate semialdehyde results only in uncoupled turnover of malonyl-CoA.
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2005
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| Summary: | Carboxymethylproline synthase was shown to condense L-glutamate semialdehyde with malonyl-coenzyme A to produce (2S,5S)-carboxymethylproline, while incubation of D-glutamate semialdehyde results only in uncoupled turnover of malonyl-CoA. |
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