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.
Autores principales: | Sorensen, J, Sleeman, M, Schofield, C |
---|---|
Formato: | Journal article |
Lenguaje: | English |
Publicado: |
2005
|
Ejemplares similares
-
Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis.
por: Sleeman, M, et al.
Publicado: (2004) -
Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis.
por: Sleeman, M, et al.
Publicado: (2005) -
Synthesis of regio- and stereoselectively deuterium-labelled derivatives of L-glutamate semialdehyde for studies on carbapenem biosynthesis.
por: Ducho, C, et al.
Publicado: (2009) -
Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC).
por: Sleeman, M, et al.
Publicado: (2004) -
Engineering carboxymethylproline synthases towards the biosynthetic productions of carbapenem antibiotics
por: Gómez Castellanos, J
Publicado: (2013)