1.14.13.101: senecionine N-oxygenase
This is an abbreviated version!
For detailed information about senecionine N-oxygenase, go to the full flat file.
Reaction
Synonyms
flavin-dependent monooxygenase, fmoa, GgPNO, oxygenase, senecionine N-, PA N-oxygenase, PNO, pyrrolizidine alkaloid N-oxygenase, senecionine monooxygenase (N-oxide-forming), senecionine N-oxygenase, SNO, TjSNO, ZvFMOa, ZvPNO
ECTree
1.14.13.101 senecionine N-oxygenaseAdvanced search results
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Engineering
Engineering on EC 1.14.13.101 - senecionine N-oxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F307Y
site-directed mutagenesis, the ZvFMOa F307Y mutation results in a decline in specific activity by a factor of 0.81 in comparison to wild-type ZvFMOa
F307Y/Y356A
site-directed mutagenesis, the ZvFMOa F307Y/Y356A double mutation results in an increase in specific activity by a factor of 1.51 in comparison to wild-type ZvFMOa
F354V
site-directed mutagenesis, the ZvFMOa F354V mutation results in an increase in specific activity by a factor of 2.75 in comparison to wild-type ZvFMOa
F354V/Y356A
site-directed mutagenesis, the ZvFMOa F354V/Y356A double mutation results in an increase in specific activity by a factor of 1.5 in comparison to wild-type ZvFMOa
P388S
site-directed mutagenesis, the specific activity of this variant does not differ significantly from that of wild-type ZvFMOa
Y356A
site-directed mutagenesis, the ZvFMOa Y356A mutation results in an increase in specific activity by a factor of 2.45 in comparison to wild-type ZvFMOa
additional information
additional information
the beneficial effect of a more accessible substrate entry path might possibly be partly antagonized by a loss of substrate affinity when both bulky aromatic amino acids are exchanged for smaller substituents. The presence of proline within the ZvFMOa helix does not interfere with its potential role in substrate turnover
additional information
the beneficial effect of a more accessible substrate entry path might possibly be partly antagonized by a loss of substrate affinity when both bulky aromatic amino acids are exchanged for smaller substituents. The presence of proline within the ZvFMOa helix does not interfere with its potential role in substrate turnover
additional information
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the beneficial effect of a more accessible substrate entry path might possibly be partly antagonized by a loss of substrate affinity when both bulky aromatic amino acids are exchanged for smaller substituents. The presence of proline within the ZvFMOa helix does not interfere with its potential role in substrate turnover
