Document Detail


Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637.
MedLine Citation:
PMID:  17077963     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
M Saito; K Nishimura; S Wakabayashi; T Kurihara; Y Nagata
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Publication Detail:
Type:  Journal Article     Date:  2006-11-02
Journal Detail:
Title:  Amino acids     Volume:  33     ISSN:  1438-2199     ISO Abbreviation:  Amino Acids     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-09-03     Completed Date:  2008-04-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  445-9     Citation Subset:  IM    
Affiliation:
Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, Tokyo, Japan.
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MeSH Terms
Descriptor/Qualifier:
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:
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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