Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione transferase P1-1.

Lin, Henry J; Johansson, Ann Sofie; Stenberg, Gun; Materi, Alicia M; Park, Jae Man; Dai, Aihua; Zhou, Haiyan; Gim, Jason S Y; Kau, Irving H; Hardy, Steven I; Parker, Michael W; Mannervik, Bengt

Lin, Henry J; Johansson, Ann Sofie; Stenberg, Gun; Materi, Alicia M; Park, Jae Man; Dai, Aihua; Zhou, Haiyan; Gim, Jason S Y; Kau, Irving H; Hardy, Steven I; Parker, Michael W; Mannervik, Bengt.

Affiliation

Lin HJ; Department of Pediatrics and the Research and Education Institute, Harbor-UCLA Medical Center, 1124 W Carson St, Torrance, CA 90502, USA. henry_lin@humc.edu

Biochim Biophys Acta ; 1649(1): 16-23, 2003 Jun 26.

Article in En | MEDLINE | ID: mdl-12818186

Subject(s)

Glutathione Transferase/chemistry; Glutathione Transferase/genetics; Isoenzymes/chemistry; Isoenzymes/genetics; Amino Acid Motifs; Amino Acid Substitution; Black People/genetics; Dinitrochlorobenzene/metabolism; Enzyme Stability/genetics; Genetic Variation; Glutathione S-Transferase pi; Glutathione Transferase/metabolism; Half-Life; Humans; Hydrophobic and Hydrophilic Interactions; Isoenzymes/metabolism; Kinetics; Leucine/genetics; Models, Molecular; Phenylalanine/genetics; Polymorphism, Genetic; Protein Folding

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Collection: 01-internacional Database: MEDLINE Main subject: Glutathione Transferase / Isoenzymes Limits: Humans Language: En Journal: Biochim Biophys Acta Year: 2003 Document type: Article

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