The Primary Structure of Bovine Monoamine Oxidase Type A. Comparison with Peptide Sequences of Bovine Monoamine Oxidase Type B and Other Flavoenzymes

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Apr 15

PMID 2719656

Citations 12

Authors

J F Powell

Y P Hsu

W Weyler

S A Chen

J SALACH

K Andrikopoulos

J Mallet

X O Breakefield

Affiliations

Soon will be listed here.

Abstract

We have isolated cDNA clones believed to encompass the full-length coding sequences for a subunit of bovine monoamine oxidase type A (MAO-A). The clones code for an apoprotein of 527 amino acid residues corresponding to a molecular mass of 59,806 Da. The inferred protein sequences show an overall similarity of 68% with partial amino acid sequences of bovine type B MAO (about 41% of the total sequence), as well as a greater similarity (greater than 90%) with some regions including that for the published sequence of the flavin-binding region. Sequence comparisons indicate that these two forms of MAO are encoded by distinct genes. Comparison of this sequence with other flavoenzymes showed similarity with regions associated with non-covalent flavin-binding sites. Analysis of mRNAs coding for MAO enzymes showed a heterogeneity of transcripts consistent with several different forms of monoamine oxidase.

Citing Articles

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