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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Oct;67(2):724–730. doi: 10.1073/pnas.67.2.724

Bovine Liver Glutamate Dehydrogenase: Tentative Amino Acid Sequence; Identification of a Reactive Lysine; Nitration of a Specific Tyrosine and Loss of Allosteric Inhibition by Guanosine Triphosphate*

Emil L Smith 1,2, Michael Landon 1,2, Dennis Piszkiewicz 1,2, William J Brattin 1,2, Trevor J Langley 1,2, Mark D Melamed 1,2
PMCID: PMC283265  PMID: 5289018

Abstract

A tentative but almost complete amino acid sequence for the subunit peptide chain of bovine liver glutamate dehydrogenase indicates a minimal size of 506 residues with a molecular weight of 56,100, in accord with the physical size of the subunit of 55,900. Inactivation with pyridoxal 5′-phosphate, followed by reduction with sodium borohydride, has permitted identification of the essential lysine as residue 97. Nitration of tyrosine-412 is accompanied by loss of the allosteric inhibitory effect of guanosine triphosphate.

Comparison of the sequences of glutamate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase has indicated that only two 12-residue sequences are similar in the two enzymes; this sequence includes reactive lysine-97 of the former enzyme.

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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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