Journal article
Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Model Structure of Protein Arginine Methyltransferase
Journal of molecular biology, Vol.320(2), pp.223-235
2002
DOI: 10.1016/S0022-2836(02)00448-5
PMID: 12079381
Abstract
Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers of all vertebrates. Recombinant rat liver GAMT has been crystallized with
Details
- Title: Subtitle
- Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Model Structure of Protein Arginine Methyltransferase
- Creators
- Junichi Komoto - Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Avenue, 2034 Howorth Hall, Lawrence, KS 66045-7534, USAYafei Huang - Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Avenue, 2034 Howorth Hall, Lawrence, KS 66045-7534, USAYoshimi Takata - Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Avenue, 2034 Howorth Hall, Lawrence, KS 66045-7534, USATaro Yamada - Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Avenue, 2034 Howorth Hall, Lawrence, KS 66045-7534, USAKiyoshi Konishi - Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama 930-0194, JapanHirofumi Ogawa - Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama 930-0194, JapanTomoharu Gomi - Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama 930-0194, JapanMotoji Fujioka - Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Sugitani, Toyama 930-0194, JapanFusao Takusagawa - Department of Molecular Biosciences, The University of Kansas, 1200 Sunnyside Avenue, 2034 Howorth Hall, Lawrence, KS 66045-7534, USA
- Resource Type
- Journal article
- Publication Details
- Journal of molecular biology, Vol.320(2), pp.223-235
- Publisher
- Elsevier Ltd
- DOI
- 10.1016/S0022-2836(02)00448-5
- PMID
- 12079381
- ISSN
- 0022-2836
- eISSN
- 1089-8638
- Language
- English
- Date published
- 2002
- Academic Unit
- Neurology
- Record Identifier
- 9984020848402771
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