Multiplicity and identity of human aldehyde dehydrogenases.
Human "high Km" aldehyde dehydrogenases have been purified to homogeneity and characterized. The "high Km" enzymes are structurally and catalytically distinct from "low Km" aldehyde dehydrogenases; they are not isozymes of the "low Km" enzymes.
Center of Alcohol Studies, Rutgers University, Piscataway, NJ 08854.
R
R
Pietruszko
M T
MT
Ryzlak
C M
CM
Forte-McRobbie
D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D001921:Brain / Q000201:enzymology; D004221:Disulfiram / Q000494:pharmacology; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology; D050644:Succinate-Semialdehyde Dehydrogenase
D007527:Isoenzymes; D000445:Aldehyde Oxidoreductases; D050644:Succinate-Semialdehyde Dehydrogenase; D000444:Aldehyde Dehydrogenase; D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D004221:Disulfiram