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IUBMB Comments Also acts on N -acetylgalactosamine and, more slowly, on N -acetylmannosamine. Anomeric specificity was tested with N -acetyl-D -glucosamine, and it was shown that the enzyme is specific for the α anomer.
Synonyms
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N-acetyl-D-hexosamine dehydrogenase
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N-acetylhexosamine dehydrogenase
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N-acetyl-alpha-D-glucosamine + NAD+ = N-acetyl-D-glucosaminate + NADH + H+
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N-acetyl-D-hexosamine:NAD+ 1-oxidoreductase
Also acts on N-acetylgalactosamine and, more slowly, on N-acetylmannosamine. Anomeric specificity was tested with N-acetyl-D-glucosamine, and it was shown that the enzyme is specific for the alpha anomer.
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N-acetyl-D-galactosamine + NAD+
N-acetyl-D-galactoseaminate + NADH
N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
N-acetyl-D-mannosamine + NAD+ + H2O
N-acetyl-D-mannosaminate + NADH + H+
N-acetyl-D-galactosamine + NAD+
N-acetyl-D-galactoseaminate + NADH
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Substrates: -
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N-acetyl-D-galactosamine + NAD+
N-acetyl-D-galactoseaminate + NADH
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Substrates: -
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N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
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Substrates: -
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N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
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Substrates: -
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N-acetyl-D-mannosamine + NAD+ + H2O
N-acetyl-D-mannosaminate + NADH + H+
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Substrates: very poor substrate
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N-acetyl-D-mannosamine + NAD+ + H2O
N-acetyl-D-mannosaminate + NADH + H+
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Substrates: very poor substrate
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N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
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Substrates: -
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N-acetyl-D-glucosamine + NAD+
N-acetyl-D-glucosaminate + NADH
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Substrates: -
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NAD+
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strictly specific for NAD+ as hydrogen acceptor
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additional information
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not effected by Ca2+, Mg2+, Cd2+, Ni2+, Zn2+, Cu2+, Mn2+, Co2+
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0.8
N-acetyl-D-galactosamine
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5.3
N-acetyl-D-glucosamine
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0.24
NAD+
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with N-acetyl-D-glucosamine as substrate
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932
N-acetyl-D-galactosamine
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655
N-acetyl-D-glucosamine
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No. 53
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brenda
No. 53
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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tetramer
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4 * 30000, SDS-PAGE, gel filtration
tetramer
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4 * 30000, SDS-PAGE, gel filtration
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45
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10 min, unstable below pH 5 and above pH 12
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10 min, 50% loss of activity
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10 min, complete loss of activity
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stabilized against heating by 3 mM NAD+
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-20°C, several months, without much loss of activity
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Horiuchi, T.; Kurokawa, T.
Purification and characterization of N-acetyl-D-hexosamine dehydrogenase from Pseudomonas sp. No. 53
Agric. Biol. Chem.
53
1919-1925
1989
Pseudomonas sp., Pseudomonas sp. No. 53
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brenda
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