Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿
Nesterenkonia strain AN1 was isolated from a screening program for nitrile- and amide-hydrolyzing microorganisms in Antarctic desert soil samples. Strain AN1 showed significant 16S rRNA sequence identity to known members of the genus. Like known Nesterenkonia species, strain AN1 was obligately alkal...
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127607 http://www.ncbi.nlm.nih.gov/pubmed/21498772 https://doi.org/10.1128/AEM.02726-10 |
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ftpubmed:oai:pubmedcentral.nih.gov:3127607 2023-05-15T13:32:03+02:00 Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ Nel, A. J. M. Tuffin, I. M. Sewell, B. T. Cowan, D. A. 2011-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127607 http://www.ncbi.nlm.nih.gov/pubmed/21498772 https://doi.org/10.1128/AEM.02726-10 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127607 http://www.ncbi.nlm.nih.gov/pubmed/21498772 http://dx.doi.org/10.1128/AEM.02726-10 Copyright © 2011, American Society for Microbiology Enzymology and Protein Engineering Text 2011 ftpubmed https://doi.org/10.1128/AEM.02726-10 2013-09-03T16:47:52Z Nesterenkonia strain AN1 was isolated from a screening program for nitrile- and amide-hydrolyzing microorganisms in Antarctic desert soil samples. Strain AN1 showed significant 16S rRNA sequence identity to known members of the genus. Like known Nesterenkonia species, strain AN1 was obligately alkaliphilic (optimum environmental pH, 9 to 10) and halotolerant (optimum environmental Na+ content, 0 to 15% [wt/vol]) but was also shown to be an obligate psychrophile with optimum growth at approximately 21°C. The partially sequenced genome of AN1 revealed an open reading frame (ORF) encoding a putative protein member of the nitrilase superfamily, referred to as NitN (264 amino acids). The protein crystallized readily as a dimer and the atomic structure of all but 10 amino acids of the protein was determined, confirming that the enzyme had an active site and a fold characteristic of the nitrilase superfamily. The protein was screened for activity against a variety of nitrile, carbamoyl, and amide substrates and was found to have only amidase activity. It had highest affinity for propionamide but demonstrated a low catalytic rate. NitN had maximal activity at 30°C and between pH 6.5 and 7.5, conditions which are outside the optimum growth range for the organism. Text Antarc* Antarctic PubMed Central (PMC) Antarctic Applied and Environmental Microbiology 77 11 3696 3702 |
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language |
English |
topic |
Enzymology and Protein Engineering |
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Enzymology and Protein Engineering Nel, A. J. M. Tuffin, I. M. Sewell, B. T. Cowan, D. A. Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
topic_facet |
Enzymology and Protein Engineering |
description |
Nesterenkonia strain AN1 was isolated from a screening program for nitrile- and amide-hydrolyzing microorganisms in Antarctic desert soil samples. Strain AN1 showed significant 16S rRNA sequence identity to known members of the genus. Like known Nesterenkonia species, strain AN1 was obligately alkaliphilic (optimum environmental pH, 9 to 10) and halotolerant (optimum environmental Na+ content, 0 to 15% [wt/vol]) but was also shown to be an obligate psychrophile with optimum growth at approximately 21°C. The partially sequenced genome of AN1 revealed an open reading frame (ORF) encoding a putative protein member of the nitrilase superfamily, referred to as NitN (264 amino acids). The protein crystallized readily as a dimer and the atomic structure of all but 10 amino acids of the protein was determined, confirming that the enzyme had an active site and a fold characteristic of the nitrilase superfamily. The protein was screened for activity against a variety of nitrile, carbamoyl, and amide substrates and was found to have only amidase activity. It had highest affinity for propionamide but demonstrated a low catalytic rate. NitN had maximal activity at 30°C and between pH 6.5 and 7.5, conditions which are outside the optimum growth range for the organism. |
format |
Text |
author |
Nel, A. J. M. Tuffin, I. M. Sewell, B. T. Cowan, D. A. |
author_facet |
Nel, A. J. M. Tuffin, I. M. Sewell, B. T. Cowan, D. A. |
author_sort |
Nel, A. J. M. |
title |
Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
title_short |
Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
title_full |
Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
title_fullStr |
Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
title_full_unstemmed |
Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate▿ |
title_sort |
unique aliphatic amidase from a psychrotrophic and haloalkaliphilic nesterenkonia isolate▿ |
publisher |
American Society for Microbiology |
publishDate |
2011 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127607 http://www.ncbi.nlm.nih.gov/pubmed/21498772 https://doi.org/10.1128/AEM.02726-10 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3127607 http://www.ncbi.nlm.nih.gov/pubmed/21498772 http://dx.doi.org/10.1128/AEM.02726-10 |
op_rights |
Copyright © 2011, American Society for Microbiology |
op_doi |
https://doi.org/10.1128/AEM.02726-10 |
container_title |
Applied and Environmental Microbiology |
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77 |
container_issue |
11 |
container_start_page |
3696 |
op_container_end_page |
3702 |
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1766023871978274816 |