Structure-function relationships of 3β-hydroxysteroid dehydrogenases involved in bile acid metabolism

Advances in Experimental Medicine and Biology

Volumn 463, Issue , 1999, Pages 389-394

  Filling, C ^a   Marschall, H U ^a   Prozorovski, T ^a   Nordling, E ^a   Persson, B ^a   Jornvall H ^a   Oppermann, U C T ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; ALCOHOL DEHYDROGENASE;

BILE ACID METABOLISM; COMAMONAS TESTOSTERONI; CONFERENCE PAPER; ENZYME ANALYSIS; ENZYME STRUCTURE; HUMAN; LIVER CYTOSOL; MOLECULAR CLONING; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

COMAMONAS TESTOSTERONI;

EID: 0033282394     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-4735-8_48     Document Type: Conference Paper

References (8)

1. The refined three-dimensional structure of 3 alpha, 20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
2. Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences
3. Short-chain dehydrogenase/reductases (SDR)
4. Human liver class I alcohol dehydrogenase γγ isozyme: The sole cytosolic 3β-hydroxysteroid dehydrogenase of iso bile acids
5. Structure-function relationships of SDR hydroxysteroid dehydrogenases
6. Active-site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on SDR reactions
7. Molecular biology and genetics of the 3-beta-hydroxysteroid dehydrogenase/delta5-delta4 isomerase gene family
8. cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family