Abstract:
:Modelling the amino acid sequence of NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase into the three-dimensional structure of 3 alpha/20 beta-hydroxysteroid dehydrogenase shows that these two enzymes, as well as the NADP(+)-linked prostaglandin dehydrogenase (identical to carbonyl reductase) have similar conformations, in spite of very limited sequence identity (23-28%). Conservation of tertiary structures is greatest over the first two thirds of the polypeptide chains, where the typical NAD+ binding fold is retained, including the five first beta-strands, with only two short deletions or insertions up to residue 147. The remaining thirds of each of the prostaglandin dehydrogenases have significantly different architecture, including insertions that may contribute to enzyme specificity, and, except for an additional helix (alpha G), are difficult to model. Active site relationships can be evaluated and subunit interactions predicted, suggesting that the alpha E + alpha F two-helix surface constitutes the major subunit interacting area, forming a dimeric unit in the oligomeric enzymes.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Krook M,Ghosh D,Duax W,Jörnvall Hdoi
10.1016/0014-5793(93)81554-dsubject
Has Abstractpub_date
1993-05-10 00:00:00pages
139-42issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(93)81554-Djournal_volume
322pub_type
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