rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2010-2-23
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pubmed:abstractText |
The high-level heterologous expression in Pichia pastoris, purification and characterization of recombinant membrane-bound rat liver monoamine oxidase A (MAO A) are described. A 1-L culture of cells produces approximately 700 U of rat MAO A activity. The rat MAO A activity is found in outer mitochondrial membrane of the cell. Using a modification of the human MAO A purification procedure, approximately 200mg of recombinant rat MAO A is purified in a 43% yield and exhibits a molecular weight of approximately 60,000 kDa on SDS-PAGE. The purified enzyme contains a covalently bound FAD and forms a N(5) flavocyanine adduct on inhibition by clorgyline. Edman sequencing shows that the amino terminus of rat MAO A is blocked at an N-terminal threonyl residue. The purified rat enzyme exhibits a higher thermal stability than does purified human MAO A. Compared with human MAO A, rat MAO A oxidizes serotonin or kynuramine with twofold higher k(cat)/K(m) values, oxidizes phenethylamine with a 6.7-fold higher catalytic efficiency and benzylamine with a approximately 40-fold higher catalytic efficiency. Although approximately 90% identical in sequence to human MAO A, rat MAO A is a more efficient catalyst for amine neurotransmitter oxidation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-10521274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-11049757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-11732903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-11753429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-11812236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-11911838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-1400344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-15050826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-15710600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-16129825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-17521909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-18391214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-2021654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-2290855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-3024631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-3069123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-3109386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-6290489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-647023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-851417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19883764-9697417
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1096-0279
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
211-7
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pubmed:dateRevised |
2011-11-14
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pubmed:meshHeading |
pubmed-meshheading:19883764-Animals,
pubmed-meshheading:19883764-Benzylamines,
pubmed-meshheading:19883764-Cloning, Molecular,
pubmed-meshheading:19883764-Enzyme Stability,
pubmed-meshheading:19883764-Humans,
pubmed-meshheading:19883764-Kinetics,
pubmed-meshheading:19883764-Monoamine Oxidase,
pubmed-meshheading:19883764-Phenethylamines,
pubmed-meshheading:19883764-Pichia,
pubmed-meshheading:19883764-Rats,
pubmed-meshheading:19883764-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:19883764-Substrate Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparison with human MAO A.
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pubmed:affiliation |
Department of Biochemistry, Emory University, Rollins Research Center, 1510 Clifton Rd., Atlanta, GA 30322, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, N.I.H., Extramural
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