SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:DiVA.org:sh-15793"
 

Search: onr:"swepub:oai:DiVA.org:sh-15793" > Critical residues f...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Filling, C (author)

Critical residues for structure and catalysis in short-chain dehydrogenases/reductases

  • Article/chapterEnglish2002

Publisher, publication year, extent ...

  • 2002
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:sh-15793
  • https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-15793URI
  • https://doi.org/10.1074/jbc.M202160200DOI
  • http://kipublications.ki.se/Default.aspx?queryparsed=id:1938030URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • Short-chain dehydrogenases/reductases form a large, evolutionarily old family of NAD(P)(H)-dependent enzymes with over 60 genes found in the human genome. Despite low levels of sequence identity (often 10-30%), the three-dimensional structures display a highly similar alpha/beta folding pattern. We have analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3beta/17beta-hydroxysteroid dehydrogenase and selected mutants. Structure determination of the wildtype enzyme at 1.2-Angstrom resolution by x-ray crystallography and docking analysis was used to interpret the biochemical data. Enzyme kinetic data from mutagenetic replacements emphasize the critical role of residues Thr-12, Asp-60, Asn-86, Asn-87, and Ala-88 in coenzyme binding and catalysis. The data also demonstrate essential interactions of Asn-111 with active site residues. A general role of its side chain interactions for maintenance of the active site configuration to build up a proton relay system is proposed. This extends the previously recognized catalytic triad of Ser-Tyr-Lys residues to form a tetrad of Asn-Ser-Tyr-Lys in the majority of characterized short-chain dehydrogenases/reductase enzymes.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Berndt, Kurt DKarolinska Institutet,Södertörns högskola,Avdelning Naturvetenskap,Karolinska Intitute(Swepub:sh)SHKTBT (author)
  • Benach, J (author)
  • Knapp, S (author)
  • Prozorovski, T (author)
  • Nordling, E (author)
  • Ladenstein, RKarolinska Institutet (author)
  • Jörnvall, HKarolinska Institutet (author)
  • Oppermann, U (author)
  • Södertörns högskolaAvdelning Naturvetenskap (creator_code:org_t)

Related titles

  • In:Journal of Biological Chemistry277:28, s. 25677-256840021-92581083-351X

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view