Three‐dimensional model of NAD+‐dependent 15‐hydroxyprostaglandin dehydrogenase and relationships to the NADP+‐dependent enzyme (carbonyl reductase)

FEBS Letters

Ghosh, Debashis¹  Krook, Maria²  Duax, William¹  Jörnvall, Hans² 

[1] Medical Foundation of Buffalo, Buffalo, NY 14203-1196, USA;Department of Chemistry I, Karolinska Institute, S-104 01 Stockholm, Sweden

关键词: Computer graphics;    Prostaglandin dehydrogenase;    Short-chain dehydrogenases;    Enzyme family;    Insertion/deletion;    Subunit interactions;   

DOI  :  10.1016/0014-5793(93)81554-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Modelling the amino acid sequence of NAD⁺-linked 15-hydroxyprostaglandin dehydrogenase into the three-dimensional structure of 3α/20β-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 β-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 (αG), are difficult to model. Active site relationships can be evaluated and subunit interactions predicted, suggesting that the αE + αF two-helix surface constitutes the major subunit interacting area, forming a dimeric unit in the oligomeric enzymes.

【 授权许可】

Unknown