Amino-Acid Sequence of NADP-Specific Glutamate Dehydrogenase of Neurospora crassa

  1. John C. Wootton*,
  2. Geoffrey K. Chambers*,
  3. Anthony A. Holder*,
  4. Andrew J. Baron*,
  5. John G. Taylor*,
  6. John R. S. Fincham*,
  7. Kenneth M. Blumenthal†,
  8. Kenneth Moon†,‡, and
  9. Emil L. Smith†
  1. *Department of Genetics, University of Leeds, Leeds LS2 9JT, U.K.
  2. †Department of Biological Chemistry, UCLA School of Medicine and Molecular Biology Institute, University of California, Los Angeles, Calif. 90024

Abstract

A tentative primary structure of the NADP-specific glutamate dehydrogenase [L-glutamate: NADP oxidoreductase (deaminating), EC 1.4.1.4] from Neurospora crassa has been determined. The proposed sequence contains 452 amino-acid residues in each of the identical subunits of the hexameric enzyme. Comparison of the sequence with that of the bovine liver enzyme reveals considerable homology in the amino-terminal portion of the chain, including the vicinity of the reactive lysine, with only shorter stretches of homology within the carboxyl-terminal regions. The significance of this distribution of homologous regions is discussed.

Footnotes

  • ↵ ‡ Present address: School of Biochemistry, University of New South Wales, Kensington 2033, Sydney, Australia.

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  1. PNAS November 1, 1974 vol. 71 no. 11 4361-4365
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