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

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Saito M, Nishimura K, Wakabayashi S, Kurihara T, Nagata Y

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

Amino Acids. 2007 Sep;33(3):445-9. Epub 2006 Nov 2.

PubMed ID

17077963 [ View in PubMed

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Abstract

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Leucine	Branched-chain-amino-acid aminotransferase, cytosolic	Protein	Humans	Unknown	Not Available	Details
Valine	Branched-chain-amino-acid aminotransferase, cytosolic	Protein	Humans	Unknown	Not Available	Details

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Valine	Branched-chain-amino-acid aminotransferase, cytosolic	Protein	Humans	Unknown	Substrate	Details