Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
We propose a multiple alignment of the sequence of formate dehydrogenase with the D-specific 2-hydroxy acid dehydrogenases family. Structurally conserved regions are predicted for those sequences corresponding to important regions of the catalytic and the coenzyme binding domains defined from the known three-dimensional structure of the formate dehydrogenase, namely the nicotinamide binding site (beta D to beta F) and the beta A-loop-alpha B region containing the typical glycine pattern of the adenosine binding site, the catalytic histidine/aspartic acid pair and an arginine probably involved in the interaction with the carboxyl group of the substrate.
Vinals
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C
Facultés Universitaires Notre Dame de la Paix, Department of Biology, Namur, Belgium.
Depiereux
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Feytmans
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E
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D002384:Catalysis; D017124:Conserved Sequence; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D007770:L-Lactate Dehydrogenase; D045022:Lactate Dehydrogenases; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D000429:Alcohol Oxidoreductases; D045022:Lactate Dehydrogenases; D007770:L-Lactate Dehydrogenase; C071195:D-lactate dehydrogenase; C021379:D-2-hydroxyacid dehydrogenase; D005560:Formate Dehydrogenases