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Journal Article

cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties

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Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Bach, A. W. J., Lan, H. C., Johnson, D. L., Abell, C. W., Bembenek, M. F., Kwan, S. W., et al. (1988). cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proceedings of the National Academy of Sciences of the United States of America, 85(13), 4934-4938. Retrieved from http://www.pnas.org/content/85/13/4934.


Cite as: http://hdl.handle.net/21.11116/0000-0000-B846-2
Abstract
The monoamine oxidases play a vital role in the metabolism of biogenic amines in the central nervous system and in peripheral tissues. Using oligonucleotide probes derived from three sequenced peptide fragments, we have isolated cDNA clones that encode the A and B forms of monoamine oxidase and have determined the nucleotide sequences of these cDNAs. Comparison of the deduced amino acid sequences shows that the A and B forms have subunit molecular weights of 59,700 and 58,800, respectively, and have 70% sequence identity. Both sequences contain the pentapeptide Ser-Gly-Gly-Cys-Tyr, in which the obligatory cofactor FAD is covalently bound to cysteine. Based on differences in primary amino acid sequences and RNA gel blot analysis of mRNAs, the A and B forms of monoamine oxidase appear to be derived from separate genes.