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Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637

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Summary.

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 µmol/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 °C, respectively.

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Saito, M., Nishimura, K., Wakabayashi, S. et al. Purification of branched-chain amino acid aminotransferase from Helicobacter pylori NCTC 11637. Amino Acids 33, 445–449 (2007). https://doi.org/10.1007/s00726-006-0452-5

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  • DOI: https://doi.org/10.1007/s00726-006-0452-5

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