Directed Evolution of the Enzyme Monoamine Oxidase (MAO-N): Highly Efficient Chemo-enzymatic Deracemisation of the Alkaloid (±)-Crispine A

ChemCatChem ◽  
2012 ◽  
Vol 4 (9) ◽  
pp. 1259-1261 ◽  
Author(s):  
Ian Rowles ◽  
Kirk J. Malone ◽  
Laura L. Etchells ◽  
Simon C. Willies ◽  
Nicholas J. Turner
Keyword(s):  
Monoamine Oxidase ◽  
Directed Evolution ◽  
Highly Efficient ◽  
Enzyme Monoamine Oxidase

A Clinical and Biochemical Study of Monoamine Oxidase Inhibition in Depressed Patients

1961 ◽  
Vol 107 (447) ◽  
pp. 239-243 ◽  
Author(s):  
W. G. Dewhurst ◽  
C. M. B. Pare
Keyword(s):  
Monoamine Oxidase ◽  
Clinical Application ◽  
Biochemical Study ◽  
Toxic Effects ◽  
Mao Inhibitors ◽  
Monoamine Oxidase Inhibition ◽  
Depressed Patients ◽  
Depressant Action ◽  
Oxidase Inhibition ◽  
Enzyme Monoamine Oxidase

The discovery that iproniazid benefits certain subjects with depression, linked with the demonstration that it inhibits the enzyme monoamine oxidase (MAO), led to the hypothesis that inhibition of MAO was the essential mechanism by which iproniazid caused relief of symptoms (Pletscher, 1959). Iproniazid, unfortunately, can produce serious toxic effects, particularly on the liver (Pare and Sandler, 1959), and this has limited its clinical application. For this reason a search has been made for MAO inhibitors with an effective anti-depressant action yet without the serious toxic effects of iproniazid. Among the newer compounds for which such claims have been made is N-isonicotinoyl (-N-N-benzylcarboxamidoethyl) hydrazine or Nialamide.

The Structure of Monoamine Oxidase from Aspergillus niger Provides a Molecular Context for Improvements in Activity Obtained by Directed Evolution

2008 ◽  
Vol 384 (5) ◽  
pp. 1218-1231 ◽  
Author(s):  
Kate E. Atkin ◽  
Renate Reiss ◽  
Valentin Koehler ◽  
Kevin R. Bailey ◽  
Sam Hart ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Monoamine Oxidase ◽  
Directed Evolution ◽  
Molecular Context

scholarly journals Ultra-high throughput functional enrichment of large monoamine oxidase (MAO-N) libraries by fluorescence activated cell sorting

The Analyst ◽  
2018 ◽  
Vol 143 (19) ◽  
pp. 4747-4755 ◽  
Author(s):  
Joanna C. Sadler ◽  
Andrew Currin ◽  
Douglas B. Kell
Keyword(s):  
Monoamine Oxidase ◽  
Directed Evolution ◽  
High Throughput ◽  
Cell Sorting ◽  
Oxidase Activity ◽  
Functional Enrichment ◽  
High Throughput Screen ◽  
Fluorescence Activated Cell Sorting ◽  
E Coli

A novel ultra-high throughput screen forin vivodetection of oxidase activity inE. colicells and its application to directed evolution.

Isoflavones prevent oxidative stress and inhibit the activity of the enzyme monoamine oxidase in vitro

2019 ◽  
Vol 46 (2) ◽  
pp. 2285-2292 ◽  
Author(s):  
Izaviany da Silva Schmitz ◽  
Larissa Finger Schaffer ◽  
Alcindo Busanello ◽  
Catiuscia Molz de Freitas ◽  
Roselei Fachinetto ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Monoamine Oxidase ◽  
Enzyme Monoamine Oxidase

Monoamine oxidase-A targeting probe for prostate cancer imaging and inhibition of metastasis

2019 ◽  
Vol 55 (88) ◽  
pp. 13267-13270 ◽  
Author(s):  
Won Young Kim ◽  
Miae Won ◽  
Abbas Salimi ◽  
Amit Sharma ◽  
Jong Hyeon Lim ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Monoamine Oxidase ◽  
Cancer Imaging ◽  
Monoamine Oxidase A ◽  
Mitochondrial Enzyme ◽  
Mao A ◽  
Enzyme Monoamine Oxidase

Mitochondrial enzyme monoamine oxidase (MAO-A) is known to be overexpressed in prostate cancer (PCa) cells.

Developmental Aspects of the Monoamine-Degrading Enzyme Monoamine Oxidase

1992 ◽  
Vol 18 (3-4) ◽  
pp. 191-200 ◽  
Author(s):  
M. Strolin Benedetti ◽  
P. Dosiert ◽  
K.F. Tipton
Keyword(s):  
Monoamine Oxidase ◽  
Degrading Enzyme ◽  
Enzyme Monoamine Oxidase

Interrelationship between the inhibition of the activity of the enzyme monoamine oxidase and the anesthetizing activity of certain compounds

1977 ◽  
Vol 11 (2) ◽  
pp. 195-198
Author(s):  
V. Ya. Grinshtein ◽  
A. A. Prikulis ◽  
B. A. Grinberga ◽  
Ya. Ya. Shusters ◽  
A. P. Skutelis
Keyword(s):  
Monoamine Oxidase ◽  
Enzyme Monoamine Oxidase

scholarly journals Recent progress in directed evolution of stereoselective monoamine oxidases

2019 ◽  
Vol 6 (1) ◽  
Author(s):  
Jiaqi Duan ◽  
Beibei Li ◽  
Youcai Qin ◽  
Yijie Dong ◽  
Jie Ren ◽  
...  
Keyword(s):  
Amino Acid ◽  
Monoamine Oxidase ◽  
Directed Evolution ◽  
Recent Progress ◽  
Acid Oxidase ◽  
Tertiary Amines ◽  
Amino Acid Oxidase ◽  
Monoamine Oxidases ◽  
The Subject ◽  
Low Activity

Abstract Monoamine oxidases (MAOs) use molecular dioxygen as oxidant to catalyze the oxidation of amines to imines. This type of enzyme can be employed for the synthesis of primary, secondary, and tertiary amines by an appropriate deracemization protocol. Consequently, MAOs are an attractive class of enzymes in biocatalysis. However, they also have limitations in enzyme-catalyzed processes due to the often-observed narrow substrate scope, low activity, or poor/wrong stereoselectivity. Therefore, directed evolution was introduced to eliminate these obstacles, which is the subject of this review. The main focus is on recent efforts concerning the directed evolution of four MAOs: monoamine oxidase (MAO-N), cyclohexylamine oxidase (CHAO), D-amino acid oxidase (pkDAO), and 6-hydroxy-D-nicotine oxidase (6-HDNO).

scholarly journals Enzymatic oxidation of substituted tryptamines catalysed by monoamine oxidase

Nukleonika ◽  
2014 ◽  
Vol 59 (3) ◽  
pp. 91-95 ◽  
Author(s):  
Sylwia Dragulska ◽  
Marianna Kańska
Keyword(s):  
Monoamine Oxidase ◽  
Isotope Effects ◽  
Kinetic Studies ◽  
Monoamine Oxidase A ◽  
Enzymatic Oxidation ◽  
Mao A ◽  
Deuterium Isotope Effects ◽  
Enzymatic Decarboxylation ◽  
Enzyme Monoamine Oxidase

Abstract The enzymatic deamination of 5-fl uorotryptamine and 5-hydroxytryptamine, 5-HT, catalysed by enzyme monoamine oxidase A (MAO-A, EC 1.4.3.4) was investigated using the kinetic (KIE) and solvent (SIE) isotope effects methods. The numerical values of deuterium isotope effects in the (1R) positions of 5-F-tryptamine were determined using non-competitive spectrophotomeric method. Isotopologue 5-F-[(1R)- -2H]-tryptamine, needed for kinetic studies was obtained by enzymatic decarboxylation of 5´-fl uoro-L-tryptophan, 5´-F-L-Trp, in fully deuteriated medium.

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