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N Use By Plants
Nitrate Assimilation
Ammonia Assimilation
Glu, Gln, Asn, Gly, Ser
Aminotransferases
Asp, Ala, GABA
Val, Leu, Ileu, Thr, Lys
Pro, Arg, Orn
Polyamines
Non-protein AAs
Alkaloids
Sulfate Assimilation
Cys, Met, AdoMet, ACC
His, Phe, Tyr, Tryp
Secondary Products
Onium Compounds
Enzymes
Methods
Simulation
References
HORT640 - Metabolic Plant Physiology

Aminotransferase Reactions

Three Dimensional Structure of Aspartate Aminotransferase

The image(s) below show the chicken heart, mitochondrial aspartate aminotransferase homodimer [EC 2.6.1.1], with the two subunits shown in blue and yellow. Notice how the two polypetide chains clasp each other. The active site lysine residues (LYS 258) (one on each subunit) are shown in red, with the coenzyme (pyridoxal phosphate) (PLP 258) shown in white. Certain residues (TYR 70, ARG 292, SER 296, ASN 297) of one subunit contribute to the active site of the other [not shown]. Therefore, the enzyme is inactive as a monomer. Image(s) were obtained using the Glaxo Wellcome Experimental Research Swiss-Pdb Viewer (v3.6b3) (see references below), using AATM_CHICK P00508 as data source.



    Guex, N., Diemand, A. and Peitsch, M.C. (1999)
    Protein modelling for all.
    TiBS 24: 364-367.

    Guex, N. and Peitsch, M. C. (1997)
    SWISS-MODEL and the Swiss-PdbViewer: An environment for
    comparative protein modelling.
    Electrophoresis 18: 2714-2723.

    Peitsch, M. C. (1995)
    Protein modeling by E-mail
    Bio/Technology 13: 658-660.

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David Rhodes
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Last Update: 10/01/09