1.2.1.92: 3,6-anhydro-alpha-L-galactose dehydrogenase
This is an abbreviated version!
For detailed information about 3,6-anhydro-alpha-L-galactose dehydrogenase, go to the full flat file.
Reaction
Synonyms
3,6-anhydro-L-galactose dehydrogenase, AHG dehydrogenase, AHGD, anhydrogalactose dehydrogenase, SCO3486, VejAHGD, VvAHGD
ECTree
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Reaction
Reaction on EC 1.2.1.92 - 3,6-anhydro-alpha-L-galactose dehydrogenase
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3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O = 3,6-anhydro-L-galactonate + NAD(P)H + H+
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3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O = 3,6-anhydro-L-galactonate + NAD(P)H + H+
catalytic mechanism, detailed overview. The catalytic process of VvAHGD involves both the two catalytic residues, Cys282 and Glu248, which not only undergo conformational changes but also function as gatekeepers between the cofactor channel and the substrate channel. The conformational changes of Cys282 and Glu248 lead to the connection and interruption of the cofactor channel and the substrate channel, which promotes the productive binding of NADPþ/L-AHG and the efficient release of NADPH and L-AHGA during the catalysis and therefore leads to the high catalytic activity of VvAHGD
3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O = 3,6-anhydro-L-galactonate + NAD(P)H + H+
catalytic mechanism, detailed overview. The catalytic process of VvAHGD involves both the two catalytic residues, Cys282 and Glu248, which not only undergo conformational changes but also function as gatekeepers between the cofactor channel and the substrate channel. The conformational changes of Cys282 and Glu248 lead to the connection and interruption of the cofactor channel and the substrate channel, which promotes the productive binding of NADPþ/L-AHG and the efficient release of NADPH and L-AHGA during the catalysis and therefore leads to the high catalytic activity of VvAHGD
Vibrio variabilis JCM 19239
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