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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… Expand
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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… Expand
2000
2000
The conversion of L-threonine to glycine in both prokaryotes and eukaryotes takes place through a two-step biochemical pathway… Expand
Highly Cited
1993
Highly Cited
1993
The nucleotide sequences of the Rhodobacter sphaeroides hemA and hemT genes, encoding 5-aminolevulinic acid (ALA) synthase… Expand
1993
1993
The enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A (CoA) lyase are known to catalyze the net conversion… Expand
1993
1993
2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for… Expand
Highly Cited
1992
Highly Cited
1992
The leucine-responsive regulatory protein (Lrp) has been shown to regulate, either positively or negatively, the transcription of… Expand
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Highly Cited
1991
Highly Cited
1991
The existence of auxotrophic mutants of Saccharomyces cerevisiae having an absolute requirement for the long-chain base (lcb… Expand
1990
1990
Pure 2-amino-3-ketobutyrate CoA ligase from Escherichia coli, which catalyzes the cleavage/condensation reaction between 2-amino… Expand
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1987
1987
Starting with 100 g (wet weight) of a mutant of Escherichia coli K-12 forced to grow on L-threonine as sole carbon source, we… Expand