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. 1974 Nov;71(11):4361–4365. doi: 10.1073/pnas.71.11.4361

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

John C Wootton *, Geoffrey K Chambers *, Anthony A Holder *, Andrew J Baron *, John G Taylor *, John R S Fincham *, Kenneth M Blumenthal †, Kenneth Moon †,‡, Emil L Smith †
PMCID: PMC433883  PMID: 4155068

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.

Keywords: homology with vertebrate enzymes

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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