A structural explanation for the retinal specificity of class 1 ALDH enzymes.
Moore
S A
SA
Institute of Molecular Biosciences, Massey University, Palmerston North, New Zealand.
Baker
H M
HM
Blythe
T J
TJ
Kitson
K E
KE
Kitson
T M
TM
Baker
E N
EN
D000444:Aldehyde Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D000080924:Aldehyde Dehydrogenase 1 Family; D000071396:Aldehyde Dehydrogenase, Mitochondrial; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D018360:Crystallography, X-Ray; D018698:Glutamic Acid / Q000737:chemistry; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D011487:Protein Conformation; D050697:Retinal Dehydrogenase; D012172:Retinaldehyde / Q000378:metabolism*; D012756:Sheep; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D007527:Isoenzymes; D009243:NAD; D018698:Glutamic Acid; D000080924:Aldehyde Dehydrogenase 1 Family; C096127:ALDH2 protein, human; D000444:Aldehyde Dehydrogenase; D000071396:Aldehyde Dehydrogenase, Mitochondrial; C510223:ALDH1A1 protein, human; D050697:Retinal Dehydrogenase; D012172:Retinaldehyde