Different segment similarities in long-chain dehydrogenases.
Long-chain dehydrogenases were scrutinized for common patterns. Overall molecular similarities are not discerned, in contrast to the situation for several short-chain and medium-chain dehydrogenases, but coenzyme-binding segments are discernible. Species variants of glucose-6-phosphate dehydrogenase reveal about 20% strictly conserved residues, grouped into three segments and supporting assignments of sites for coenzyme-binding and catalysis. Glycine is overrepresented among the residues conserved, typical of distantly related proteins. Two of the enzymes within the pentose phosphate pathway reveal a distant similarity of interest for further evaluation, between a C-terminal 178-residue segment of glucose-6-phosphate dehydrogenase and the N-terminal part of 6-phosphogluconate dehydrogenase.
Persson
B
B
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Jeffery
J
J
Jörnvall
H
H
D000595:Amino Acid Sequence; D001665:Binding Sites; D003067:Coenzymes / Q000378:metabolism; D016208:Databases, Factual; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid
D003067:Coenzymes; D010088:Oxidoreductases