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          Institute: MPI für medizinische Forschung     Collection: Abteilung Molekulare Neurobiologie     Display Documents

ID: 22182.0, MPI für medizinische Forschung / Abteilung Molekulare Neurobiologie
cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties
Translation of Title:cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties
Authors:Bach, Alfred; Lan, H. C.; Johnson, D. L.; Abell, C. W.; Bembenek, M. F.; Kwan, S. W.; Seeburg, Peter H.; Shih, J. C.
Date of Publication (YYYY-MM-DD):1988
Title of Journal:PNAS Online 1990 - Present
Journal Abbrev.:Proc. Natl. Acad. Sci. U. S. A.
Issue / Number:13
Start Page:4943
End Page:4938
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Molekulare Neurobiologie/
Identifiers:URI:http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... [Abstract]
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