2-amino-3-ketobutyrate

Known as: 2-AKBT 
 

Topic mentions per year

Topic mentions per year

1977-2017
01219772017

Papers overview

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2002
2002
L-threonine is an indispensable amino acid. One of the major L-threonine degradation pathways is the conversion of L-threonine… (More)
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2002
2002
In mammals, L-threonine is an indispensable amino acid. The conversion of L-threonine to glycine occurs through a two-step… (More)
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2001
2001
2-Amino-3-ketobutyrate CoA ligase (KBL, EC 2.3.1.29) is a pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the second… (More)
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2000
2000
The conversion of L-threonine to glycine in both prokaryotes and eukaryotes takes place through a two-step biochemical pathway… (More)
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1993
1993
The enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A (CoA) lyase are known to catalyze the net conversion… (More)
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1993
1993
2-Amino-3-ketobutyrate ligase catalyzes the reversible, pyridoxal 5'-phosphate-dependent condensation of glycine with acetyl CoA… (More)
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1993
1993
2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for… (More)
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1991
1991
The existence of auxotrophic mutants of Saccharomyces cerevisiae having an absolute requirement for the long-chain base (lcb… (More)
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1990
1990
Pure 2-amino-3-ketobutyrate CoA ligase from Escherichia coli, which catalyzes the cleavage/condensation reaction between 2-amino… (More)
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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… (More)
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