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Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2000 (English)In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ISSN 0006-291X, Vol. 271, no 1, 59-63 p.Article in journal (Refereed) Published
Abstract [en]

The dimer interface in human GSTP1-1 has been altered by site-directed mutagenesis of Tyr50. It is shown that the effects of some mutations of this single amino acid residue are as detrimental for enzyme function as mutations of Tyr8 in the active site. T

Place, publisher, year, edition, pages
ACADEMIC PRESS INC , 2000. Vol. 271, no 1, 59-63 p.
Keyword [en]
glutathione transferases; structural motifs; mutagenesis; subunit interactions; catalysis; S-TRANSFERASE; CLASS-PI; 3-DIMENSIONAL STRUCTURE; POSITIVE COOPERATIVITY; CRYSTAL-STRUCTURE; HYDROPHOBIC CORE; HUMAN PLACENTA; ACTIVE-SITE; MECHANISM; COMPLEX
Identifiers
URN: urn:nbn:se:uu:diva-37997OAI: oai:DiVA.org:uu-37997DiVA: diva2:65896
Note
Addresses: Stenberg G, 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

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