Novel Route for Agmatine Catabolism in Aspergillus niger Involves 4-Guanidinobutyrase
DSpace at IIT Bombay
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Title |
Novel Route for Agmatine Catabolism in Aspergillus niger Involves 4-Guanidinobutyrase
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Creator |
KUMAR, S
SARAGADAM, T PUNEKAR, NS |
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Subject |
BIOSYNTHETIC ARGININE DECARBOXYLASE
SUCCINIC SEMIALDEHYDE DEHYDROGENASE PSEUDOMONAS-AERUGINOSA POLYAMINE BIOSYNTHESIS PYRROLOQUINOLINE QUINONE SACCHAROMYCES-CEREVISIAE PENICILLIUM ROQUEFORTI ESCHERICHIA-COLI AMINE OXIDASE ARGINASE |
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Description |
Agmatine, a significant polyamine in bacteria and plants, mostly arises from the decarboxylation of arginine. The functional importance of agmatine in fungi is poorly understood. The metabolism of agmatine and related guanidinium group-containing compounds in Aspergillus niger was explored through growth, metabolite, and enzyme studies. The fungus was able to metabolize and grow on L-arginine, agmatine, or 4-guanidinobutyrate as the sole nitrogen source. Whereas arginase defined the only route for arginine catabolism, biochemical and bioinformatics approaches suggested the absence of arginine decarboxylase in A. niger. Efficient utilization by the parent strain and also by its arginase knockout implied an arginase-independent catabolic route for agmatine. Urea and 4-guanidinobutyrate were detected in the spent medium during growth on agmatine. The agmatine-grown A. niger mycelia contained significant levels of amine oxidase, 4-guanidinobutyraldehyde dehydrogenase, 4-guanidinobutyrase (GBase), and succinic semialdehyde dehydrogenase, but no agmatinase activity was detected. Taken together, the results support a novel route for agmatine utilization in A. niger. The catabolism of agmatine by way of 4-guanidinobutyrate to 4-aminobutyrate into the Krebs cycle is the first report of such a pathway in any organism. A. niger GBase peptide fragments were identified by tandem mass spectrometry analysis. The corresponding open reading frame from the A. niger NCIM 565 genome was located and cloned. Subsequent expression of GBase in both Escherichia coli and A. niger along with its disruption in A. niger functionally defined the GBase locus (gbu) in the A. niger genome.
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Publisher |
AMER SOC MICROBIOLOGY
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Date |
2016-01-15T09:49:10Z
2016-01-15T09:49:10Z 2015 |
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Type |
Article
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Identifier |
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 81(16)5593-5603
0099-2240 1098-5336 http://dx.doi.org/10.1128/AEM.03987-14 http://dspace.library.iitb.ac.in/jspui/handle/100/18293 |
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Language |
en
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