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2-amino-3-ketobutyrate

Known as: 2-AKBT 
National Institutes of Health

Papers overview

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Highly Cited
2002
Highly Cited
2002
  • A. Edgar
  • BMC Genetics
  • 2002
  • Corpus ID: 310875
BackgroundL-threonine is an indispensable amino acid. One of the major L-threonine degradation pathways is the conversion of L… 
Highly Cited
2001
Highly Cited
2001
2-Amino-3-ketobutyrate CoA ligase (KBL, EC 2.3.1.29) is a pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the second… 
2000
2000
The conversion of L-threonine to glycine in both prokaryotes and eukaryotes takes place through a two-step biochemical pathway… 
1993
1993
The enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A (CoA) lyase are known to catalyze the net conversion… 
Highly Cited
1993
Highly Cited
1993
The nucleotide sequences of the Rhodobacter sphaeroides hemA and hemT genes, encoding 5-aminolevulinic acid (ALA) synthase… 
1993
1993
2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for… 
Highly Cited
1992
Highly Cited
1992
The leucine-responsive regulatory protein (Lrp) has been shown to regulate, either positively or negatively, the transcription of… 
Highly Cited
1991
Highly Cited
1991
The existence of auxotrophic mutants of Saccharomyces cerevisiae having an absolute requirement for the long-chain base (lcb…