Cloning and Characterization of a 4-Hydroxyphenylacetate 3-Hydroxylase From the Thermophile Geobacillus sp. PA-9

A 4-hydroxyphenylacetic acid (4-HPA) hydroxylase-encoding gene, on a 2.7-kb genomic DNA fragment, was cloned from the thermophile Geobacillus sp. PA-9. The Geobacillus sp. PA-9 4-HPA hydroxylase gene, designated hpaH, encodes a protein of 494 amino acids with a predicted molecular mass of 56.269 Da....

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Published in:Current microbiology 2007-12, Vol.55 (6), p.480-484
Main Authors: Hawumba, J. F, Brözel, V. S, Theron, J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Arthrobacter globiformis
Bacillaceae - enzymology
Bacillaceae - genetics
Bacillaceae - growth & development
Bacteria
Cloning
Cloning, Molecular
Deoxyribonucleic acid
DNA
DNA, Bacterial - analysis
DNA, Bacterial - isolation & purification
E coli
Enzymes
Escherichia coli
Geobacillus
Klebsiella pneumoniae
Microbiology
Mixed Function Oxygenases - chemistry
Mixed Function Oxygenases - genetics
Mixed Function Oxygenases - metabolism
Molecular Sequence Data
Phenylacetates - metabolism
Sequence Alignment
Sequence Analysis, DNA
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description A 4-hydroxyphenylacetic acid (4-HPA) hydroxylase-encoding gene, on a 2.7-kb genomic DNA fragment, was cloned from the thermophile Geobacillus sp. PA-9. The Geobacillus sp. PA-9 4-HPA hydroxylase gene, designated hpaH, encodes a protein of 494 amino acids with a predicted molecular mass of 56.269 Da. The deduced amino-acid sequence of the hpaH gene product displayed
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PA-9</title><source>Springer Nature</source><creator>Hawumba, J. F ; Brözel, V. S ; Theron, J</creator><creatorcontrib>Hawumba, J. F ; Brözel, V. S ; Theron, J</creatorcontrib><description>A 4-hydroxyphenylacetic acid (4-HPA) hydroxylase-encoding gene, on a 2.7-kb genomic DNA fragment, was cloned from the thermophile Geobacillus sp. PA-9. The Geobacillus sp. PA-9 4-HPA hydroxylase gene, designated hpaH, encodes a protein of 494 amino acids with a predicted molecular mass of 56.269 Da. The deduced amino-acid sequence of the hpaH gene product displayed &lt;30% amino-acid sequence identity with the larger monooxygenase components of the previously characterized two-component 4-HPA 3-hydroxylases from Escherichia coli W and Klebsiella pneumoniae M5a1. A second oxidoreductase component was not present on the 2.7-kb genomic DNA fragment. The deduced amino-acid sequence of a second C-terminal truncated open reading frame, designated hpaI, exhibited homology to extradiol oxygenases and displayed the highest amino-acid sequence identity (43%) with the 3,4-dihydroxyphenylacetate 2,3-dioxygenase of Arthrobacter globiformis, encoded by mndD. These results, along with catalytic activity observed in crude intracellular extracts prepared from Escherichia coli cells expressing hpaH, is in support of a role for hpaH in the 4-HPA degradative pathway of Geobacillus sp. 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F</creatorcontrib><creatorcontrib>Brözel, V. S</creatorcontrib><creatorcontrib>Theron, J</creatorcontrib><title>Cloning and Characterization of a 4-Hydroxyphenylacetate 3-Hydroxylase From the Thermophile Geobacillus sp. PA-9</title><title>Current microbiology</title><addtitle>Curr Microbiol</addtitle><description>A 4-hydroxyphenylacetic acid (4-HPA) hydroxylase-encoding gene, on a 2.7-kb genomic DNA fragment, was cloned from the thermophile Geobacillus sp. PA-9. The Geobacillus sp. PA-9 4-HPA hydroxylase gene, designated hpaH, encodes a protein of 494 amino acids with a predicted molecular mass of 56.269 Da. The deduced amino-acid sequence of the hpaH gene product displayed &lt;30% amino-acid sequence identity with the larger monooxygenase components of the previously characterized two-component 4-HPA 3-hydroxylases from Escherichia coli W and Klebsiella pneumoniae M5a1. A second oxidoreductase component was not present on the 2.7-kb genomic DNA fragment. 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F</au><au>Brözel, V. S</au><au>Theron, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Characterization of a 4-Hydroxyphenylacetate 3-Hydroxylase From the Thermophile Geobacillus sp. PA-9</atitle><jtitle>Current microbiology</jtitle><addtitle>Curr Microbiol</addtitle><date>2007-12-01</date><risdate>2007</risdate><volume>55</volume><issue>6</issue><spage>480</spage><epage>484</epage><pages>480-484</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><abstract>A 4-hydroxyphenylacetic acid (4-HPA) hydroxylase-encoding gene, on a 2.7-kb genomic DNA fragment, was cloned from the thermophile Geobacillus sp. PA-9. The Geobacillus sp. PA-9 4-HPA hydroxylase gene, designated hpaH, encodes a protein of 494 amino acids with a predicted molecular mass of 56.269 Da. The deduced amino-acid sequence of the hpaH gene product displayed &lt;30% amino-acid sequence identity with the larger monooxygenase components of the previously characterized two-component 4-HPA 3-hydroxylases from Escherichia coli W and Klebsiella pneumoniae M5a1. A second oxidoreductase component was not present on the 2.7-kb genomic DNA fragment. The deduced amino-acid sequence of a second C-terminal truncated open reading frame, designated hpaI, exhibited homology to extradiol oxygenases and displayed the highest amino-acid sequence identity (43%) with the 3,4-dihydroxyphenylacetate 2,3-dioxygenase of Arthrobacter globiformis, encoded by mndD. These results, along with catalytic activity observed in crude intracellular extracts prepared from Escherichia coli cells expressing hpaH, is in support of a role for hpaH in the 4-HPA degradative pathway of Geobacillus sp. PA-9.</abstract><cop>United States</cop><pub>New York : Springer-Verlag</pub><pmid>17805928</pmid><doi>10.1007/s00284-007-9016-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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ispartof Current microbiology, 2007-12, Vol.55 (6), p.480-484
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source Springer Nature
subjects Amino Acid Sequence
Amino acids
Arthrobacter globiformis
Bacillaceae - enzymology
Bacillaceae - genetics
Bacillaceae - growth & development
Bacteria
Cloning
Cloning, Molecular
Deoxyribonucleic acid
DNA
DNA, Bacterial - analysis
DNA, Bacterial - isolation & purification
E coli
Enzymes
Escherichia coli
Geobacillus
Klebsiella pneumoniae
Microbiology
Mixed Function Oxygenases - chemistry
Mixed Function Oxygenases - genetics
Mixed Function Oxygenases - metabolism
Molecular Sequence Data
Phenylacetates - metabolism
Sequence Alignment
Sequence Analysis, DNA
title Cloning and Characterization of a 4-Hydroxyphenylacetate 3-Hydroxylase From the Thermophile Geobacillus sp. PA-9
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