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1.1.99.29: pyranose dehydrogenase (acceptor)

This is an abbreviated version!
For detailed information about pyranose dehydrogenase (acceptor), go to the full flat file.

Word Map on EC 1.1.99.29

Reaction

a pyranose
+
acceptor
=
a pyranos-2-ulose (or a pyranos-3-ulose or a pyranos-2,3-diulose)
 +
reduced acceptor

Synonyms

AbPDH1, dehydrogenase, pyranose 2/3-, PDH, PDH AM, PDH AX, PDH1, PDH2, PDH3, pyranose 2-dehydrogenase, pyranose 2/3-dehydrogenase, pyranose 3-dehydrogenase, pyranose dehydrogenase, pyranose dehydrogenase 1, pyranose dehydrogenase 2, pyranose dehydrogenase 3, pyranose-quinone oxidoreductase, pyranose/acceptor oxidoreductase, pyranose:acceptor oxidoreductase, pyranose:quinone acceptor 2-oxidoreductase, quinone-dependent pyranose dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                1.1.99.29 pyranose dehydrogenase (acceptor)

Engineering

Engineering on EC 1.1.99.29 - pyranose dehydrogenase (acceptor)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H103A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
H103Y
H512A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100000 compared to the wild type enzyme
H556A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme
H556N
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 1000 compared to the wild type enzyme
N175Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N175Q/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G/N175Q/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
N75G/N252Q
N-glycosylation site knock out mutant with reduced activity compares to the wild type enzyme
Q392A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
V511F
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme
V511W
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 10 compared to the wild type enzyme
Y510A
the mutant shows a reduction in catalytic efficiency for glucose by a factor of 100 compared to the wild type enzyme