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Cited by 288

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Structural adaptations of lactate dehydrogenase isozymes.

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Eventoff, W, Rossmann, M G, Taylor, S S, Torff, H J, Meyer, H, Keil, W, Kiltz, H H·1977·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Eventoff, W., Rossmann, M. G., Taylor, S. S., Torff, H. J., Meyer, H., Keil, W., & Kiltz, H. H.
Venue
Proceedings of the National Academy of Sciences
Published
1977-07
Volume
74
Issue
7
Pages
2677-2681
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1963967386
Cited by
288
References
0
FWCI
18.19
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Structural adaptations of lactate dehydrogenase isozymes. https://app.cochat.ai/papers/10.1073/pnas.74.7.2677
The paper
Eventoff, W., Rossmann, M. G., Taylor, S. S., Torff, H. J., Meyer, H., Keil, W., & Kiltz, H. H. (1977). Structural adaptations of lactate dehydrogenase isozymes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.7.2677

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