Structural adaptations of lactate dehydrogenase isozymes.

Authors:
  • WEW Eventoff
    W Eventoff
  • MRM G Rossmann
    M G Rossmann
  • STS S Taylor
    S S Taylor
  • HTH J Torff
    H J Torff
  • HMH Meyer
    H Meyer
  • WKW Keil
    W Keil
  • HKH H Kiltz
    H H Kiltz
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Abstract
The three-dimensional structures of dogfish M4 (muscle) and pig H4 (heart) lactate dehydrogenase (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) have been determined and correlated with the amino acid sequences of the dogfish M4, pig M4, pig H4, chicken M4, and chicken H4 lactate dehydrogenase isozymes. These results have been related to the known differences of physicochemical properties between the M and H lactate dehydrogenase isozymes. By far the largest structural alterations occur in the transition between the "apo" and "ternary complex" conformational states of the enzyme rather than between species or isozymes. The major catalytic difference can be explained by a replacement of alanine (in the M chain) with a glutamine (in the H chain) in the vicinity of the binding site of the coenzyme phosphates. The known immunological differentiation of the M and H isozymes is consistent with the differences in their amino acid sequences.

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