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Q38317161-5E8D38CE-16B1-44E2-BD9E-51AA69F0B9DB
Q38317161-5E8D38CE-16B1-44E2-BD9E-51AA69F0B9DB
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http://www.wikidata.org/entity/statement/Q38317161-5E8D38CE-16B1-44E2-BD9E-51AA69F0B9DB
A double residue substitution in the coenzyme-binding site accounts for the different kinetic properties between yeast and human formaldehyde dehydrogenases.
P2860
Q38317161-5E8D38CE-16B1-44E2-BD9E-51AA69F0B9DB
BestRank
Statement
http://www.wikidata.org/entity/statement/Q38317161-5E8D38CE-16B1-44E2-BD9E-51AA69F0B9DB
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wasDerivedFrom
7377dc7e24c3f787867963a7ce9fde0c7bada9d0
P2860
Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase