| Literature DB >> 2043108 |
B Persson1, J Jeffery, H Jörnvall.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1991 PMID: 2043108 DOI: 10.1016/0006-291x(91)91970-n
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575