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Journal article

Clarification of the role of key active site residues of glutathione transferase Zeta/maleylacetoacetate isomerase by a new spectrophotometric technique

PG Board, MC Taylor, M Coggan, MW Parker, HB Lantum, MW Anders

Biochemical Journal | PORTLAND PRESS | Published : 2003

DOI: 10.1042/BJ20030625

University of Melbourne Researchers

Michael Parker's Profile Picture
Michael Parker Author Biochemistry and Pharmacology

Grants

Awarded by NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES


Awarded by NIEHS NIH HHS


Citation metrics

29Web of Science
30Scopus
36Dimensions

Keywords

Humans
Maleylacetone
Disinfection By-Products
Tyrosine Catabolism
Maleylacetate Isomerase (maai)
B6c3f1 Mice
Biochemistry & Molecular Biology
Cis-Trans-Isomerases
Catalytic Mechanism
Binding Sites
S-Transferase
Amino Acids
Dichloroacetic-Acid
Site-Directed Mutagenesis
Mutagenesis, Site-Directed
Catalysis
Zeta-Class Glutathione Transferase
Crystal-Structure
Science & Technology
Zeta
Trichloroacetic-Acid
Glutathione Transferase
Life Sciences & Biomedicine
Spectrophotometry
Gas Chromatography-Mass Spectrometry
Glutathione
Glutathione Transferase (gst)

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