uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
A highly acidic tyrosine 9 and a normally titrating tyrosine 212 contribute to the catalytic mechanism of human glutathione transferase A4-4
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2001 (English)In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ISSN 0006-291X, Vol. 280, no 3, 878-882 p.Article in journal (Refereed) Published
Abstract [en]

Human glutathione transferase A4-4 is an enzyme catalyzing the detoxication of intracellularly produced electrophiles such as 4-hydroxynonenal and other alkenal products of lipid peroxidation. Two tyrosines in the active site of the enzyme have been studi

Place, publisher, year, edition, pages
ACADEMIC PRESS INC , 2001. Vol. 280, no 3, 878-882 p.
Keyword [en]
glutathione transferase A4-4; active site; tyrosine; pK(a); ACTIVE-SITE; S-TRANSFERASE; LIPID-PEROXIDATION; A1-1; MUTAGENESIS; EFFICIENCY; PRODUCTS; RESIDUE; GST
Identifiers
URN: urn:nbn:se:uu:diva-38018OAI: oai:DiVA.org:uu-38018DiVA: diva2:65917
Note
Addresses: Hubatsch I, Uppsala Univ, Biomed Ctr, Dept Biochem, Box 576, SE-75123 Uppsala, Sweden. Uppsala Univ, Biomed Ctr, Dept Biochem, SE-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

Open Access in DiVA

No full text

By organisation
Department of Biochemistry

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 390 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf