| Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637. | |
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MedLine Citation:
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PMID: 17077963 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Branched-chain amino acid aminotransferase was purified by several column chromatographies from Helicobacter pylori NCTC 11637, and the N-terminal amino acid sequence was analyzed. The enzyme gene was sequenced based on a putative branched-chain amino acid aminotransferase gene, ilvE of H. pylori 26695, and the whole amino acid sequence was deduced from the nucleotide sequence. The enzyme existed in a homodimer with a calculated subunit molecular weight (MW) of 37,539 and an isoelectric point (pI) of 6.47. The enzyme showed high affinity to 2-oxoglutarate (K (m) = 0.085 mM) and L-isoleucine (K (m) = 0.34 mM), and V (max) was 27.3 micromol/min/mg. The best substrate was found to be L-isoleucine followed by L-leucine and L-valine. No activity was shown toward the D-enantiomers of these amino acids. The optimal pH and temperature were pH 8.0 and 37 degrees C, respectively. |
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Authors:
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M Saito; K Nishimura; S Wakabayashi; T Kurihara; Y Nagata |
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Publication Detail:
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Type: Journal Article Date: 2006-11-02 |
Journal Detail:
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Title: Amino acids Volume: 33 ISSN: 1438-2199 ISO Abbreviation: Amino Acids Publication Date: 2007 Sep |
Date Detail:
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Created Date: 2007-09-03 Completed Date: 2008-04-09 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9200312 Medline TA: Amino Acids Country: Austria |
Other Details:
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Languages: eng Pagination: 445-9 Citation Subset: IM |
Affiliation:
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Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Tokyo, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Bacterial Proteins / chemistry, genetics, isolation & purification* Helicobacter pylori / enzymology* Humans Hydrogen-Ion Concentration Isoelectric Point Ketoglutaric Acids / metabolism Molecular Sequence Data Protein Structure, Quaternary Substrate Specificity Transaminases / chemistry, genetics, isolation & purification* Valine / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Ketoglutaric Acids; 328-50-7/alpha-ketoglutaric acid; 7004-03-7/Valine; EC 2.6.1.-/Transaminases; EC 2.6.1.42/branched-chain-amino-acid transaminase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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