Literature DB >> 1764060

Differences in substrate specificities of monoamine oxidase A from human liver and placenta.

A K Tan1, W Weyler, J I Salach, T P Singer.   

Abstract

The substrate specificities of monoamine oxidase (MAO) A isolated from human placenta and of human liver expressed in yeast have been compared in homogeneous preparations with respect to Vmax and Km values for natural and synthetic substrates and Ki values for competitive inhibitors. MAO A from these two sources is known to differ in at least 5 amino acid residues. While the Km and Ki values were found to be nearly identical in the enzymes from these two sources, the Vmax differed significantly on bulky synthetic substrates.

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Year:  1991        PMID： 1764060     DOI： 10.1016/0006-291x(91)92048-o

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.

Authors:  T Z E Jones; D Balsa; M Unzeta; R R Ramsay
Journal:  J Neural Transm (Vienna)       Date:  2007-03-31       Impact factor: 3.575

Review 2.  90 years of monoamine oxidase: some progress and some confusion.

Authors:  Keith F Tipton
Journal:  J Neural Transm (Vienna)       Date:  2018-04-10       Impact factor: 3.575

3.  Inhibition of type A and B monoamine oxidase by 6,7-dihydroxy-1,2,3,4-tetrahydroisoquinolines and their N-methylated derivatives.

Authors:  M Minami; W Maruyama; P Dostert; T Nagatsu; M Naoi
Journal:  J Neural Transm Gen Sect       Date:  1993
  3 in total

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