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Betaine-homocysteine methyltransferase: zinc in a distorted barrel

  1. 1.
    0194441 - UOCHB-X 20020108 RIV GB eng J - Journal Article
    Evans, J. C. - Huddler, D. P. - Jiráček, Jiří - Castro, C. - Millian, N. S. - Garrow, T. A. - Ludwig, M. L.
    Betaine-homocysteine methyltransferase: zinc in a distorted barrel.
    Structure. Roč. 10, - (2002), s. 1159-1171. ISSN 0969-2126. E-ISSN 1878-4186
    R&D Projects: GA AV ČR IAB4055003
    Grant - others:NIH(US) GM16429; NIH(US) DK52501
    Institutional research plan: CEZ:AV0Z4055905
    Keywords : homocysteine
    Subject RIV: CE - Biochemistry
    Impact factor: 6.030, year: 2002

    In this paper we describe the structure of BHMT in the oxidized (Zn-free) and reduced (Zn-replete) states. The structure of BHMT in complex with the transition-state mimic, S(ë-carboxybutyl)-L-homocysteine, has allowed us to define the interactions that are responsible for substrate binding and specificity.
    Permanent Link: http://hdl.handle.net/11104/0090116


     
     

Number of the records: 1  

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