PROSITE: PDOC00144 (documentation file)

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# PROSITE: PDOC00144 (documentation)

    {PDOC00144}
    {PS00159; ALDOLASE_KDPG_KHG_1}
    {PS00160; ALDOLASE_KDPG_KHG_2}
    {BEGIN}
    *************************************************
    * KDPG and KHG aldolases active site signatures *
    *************************************************

    4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16)  (KHG-aldolase)  catalyzes the
    interconversion of  4-hydroxy-2-oxoglutarate  into  pyruvate  and  glyoxylate.
    Phospho-2-dehydro-3-deoxygluconate  aldolase   (EC 4.1.2.14)   (KDPG-aldolase)
    catalyzes the interconversion of  6-phospho-2-dehydro-3-deoxy-D-gluconate into
    pyruvate and glyceraldehyde 3-phosphate.

    These two enzymes are structurally and functionally related [1]. They are both
    homotrimeric proteins of approximately 220 amino-acid residues. They are class
    I aldolases whose catalytic mechanism involves  the formation of a Schiff-base
    intermediate  between  the  substrate  and the epsilon-amino group of a lysine
    residue. In both enzymes, an arginine is required for catalytic activity.

    We developed  two signature patterns for these enzymes. The first one contains
    the active  site  arginine  and the second, the lysine involved in the Schiff-
    base formation.

    -Consensus pattern: G-[LIVM]-x(3)-E-[LIV]-T-[LF]-R
                        [R is the active site residue]
    -Sequences known to belong to this class detected by the pattern: ALL,  except
     for Bacillus  subtilis  KDPG-aldolase  which  has  Thr  instead of Arg in the
     active site.
    -Other sequence(s) detected in SWISS-PROT: NONE.

    -Consensus pattern: G-x(3)-[LIVMF]-K-[LF]-F-P-[SA]-x(3)-G
                        [K is involved in Schiff-base formation]
    -Sequences known to belong to this class detected by the pattern: ALL.
    -Other sequence(s) detected in SWISS-PROT: NONE.

    -Last update: November 1997 / Patterns and text revised.

    [ 1] Vlahos C J., Dekker E.E.
         J. Biol. Chem. 263:11683-11691(1988).

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    {END}

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