FAD synthetase

Known as: FAD pyrophosphorylase, FMN adenylyltransferase 
 
National Institutes of Health

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2010
2010
FAD synthetase or ATP:FMN adenylyl transferase (FADS or FMNAT, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts… Expand
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2009
2009
In bacteria, riboflavin phosphorylation and subsequent conversion of FMN into FAD are carried out by FAD synthetase, a single… Expand
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2008
2008
BackgroundThe prokaryotic FAD synthetase family – a group of bifunctional enzymes that catalyse riboflavin phosphorylation and… Expand
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2007
2007
FAD synthetase (FADS) (EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor FAD… Expand
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2006
2006
FAD synthetase (FADS) (EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor FAD… Expand
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1998
1998
The bifunctional enzyme, FAD synthetase (FS), from Corynebacterium ammoniagenes was overproduced in Escherichia coli and purified… Expand
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1997
1997
Publisher Summary The formation of flavin adenine dinucleotide (FAD) depends on the sequential utilization of 2 mol of ATP in… Expand
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1987
1987
Flavin adenine dinucleotide synthetase (ATP:FMN adenylyltransferase, EC 2.7.7.2) was purified about 10,000-fold from the high… Expand
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1986
1986
The bifunctional enzyme FAD synthetase from Brevibacterium ammoniagenes was purified by a method involving ATP-affinity… Expand
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1979
1979
A flavokinase preparation from Bacillus subtilis is described which catalyzes the phosphorylation of reduced, but not oxidized… Expand
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