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The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. Additionally we are shipping Glycine C-Acetyltransferase Proteins (6) and many more products for this protein.
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Nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase (KBL) was detected in response to cold and osmotic stresses.
The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. This gene encodes the second enzyme in this pathway, which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The encoded enzyme is considered a class II pyridoxal-phosphate-dependent aminotransferase. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 14.
glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase)
, 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
, glycine C-acetyltransferase
, Glycine C-acetyltransferase
, glycine c-acetyltransferase
, 2-amino-3-ketobutyrate-CoA ligase
, AKB ligase
, aminoacetone synthase
, glycine acetyltransferase
, glycine C-acetyltransferase (2-amino-3-ketobutyrate-coenzyme A ligase)
, aminoacetone synthetase