Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 36, 2004, Pages 13163-13167

  Hederos, Sofia ^a   Broo, Kerstin S ^a   Jakobsson, Emma ^b   Kleywegt, Gerard J ^b   Mannervik, Bengt ^b   Baltzer, Lars ^b  

^a LINKÖPING UNIVERSITY   (Sweden)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE A1; HISTIDINE; THIOESTER; UNCLASSIFIED DRUG;

ARTICLE; CATALYST; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME KINETICS; HYDROLYSIS; PRIORITY JOURNAL; REACTION ANALYSIS; TRANSESTERIFICATION;

GLUTATHIONE TRANSFERASE; HISTIDINE; HUMANS; HYDROLYSIS; MUTAGENESIS, SITE-DIRECTED; SULFHYDRYL COMPOUNDS;

FELIS CATUS;

EID: 4444291472     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0403045101     Document Type: Article

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