1.1.99.42: 4-pyridoxic acid dehydrogenase
This is an abbreviated version!
For detailed information about 4-pyridoxic acid dehydrogenase, go to the full flat file.
Reaction
Synonyms
mlr6739, mlr6792, mlr6793
ECTree
1.1.99.42 4-pyridoxic acid dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.1.99.42 - 4-pyridoxic acid dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E149Q
mutant shows a showed a different pH optimum depending on the cosubstrate. With NAD+, the mutant shows very low activity with an optimum pH at 8.5 in the universal buffer. In contrast, the optimum pH is 5.5 with NADH
E149Q
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mutant shows a showed a different pH optimum depending on the cosubstrate. With NAD+, the mutant shows very low activity with an optimum pH at 8.5 in the universal buffer. In contrast, the optimum pH is 5.5 with NADH
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additional information
additional information
deletion or mutation of a deduced transmembrane segment in 4-pyridoxic acid dehydrogenase makes it an inclusion body upon expression in Escherichia coli, and the enzyme protein is not found in the cell membrane
additional information
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deletion or mutation of a deduced transmembrane segment in 4-pyridoxic acid dehydrogenase makes it an inclusion body upon expression in Escherichia coli, and the enzyme protein is not found in the cell membrane
additional information
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deletion or mutation of a deduced transmembrane segment in 4-pyridoxic acid dehydrogenase makes it an inclusion body upon expression in Escherichia coli, and the enzyme protein is not found in the cell membrane
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