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Article

Amino acid alterations essential for increasing the catalytic activity of the nylon-oligomer-degradation enzyme of Flavobacterium sp.

European journal of biochemistry - 15 Aug 1991

Kato K, Fujiyama K, Hatanaka H S, Priyambada I D, Negoro S, Urabe I, Okada H

Abstract excerpt

The structural genes of two homologous enzymes, 6-aminohexanoate-dimer hydrolase (EII; nylB) and its evolutionally related protein EII' (nylB') of Flavobacterium sp. KI72 have an open reading frame encoding a peptide of 392 amino acids, of which 47 are different, and conserved restriction sites. The specific activity of EII towards 6-aminohexanoate dimer is about 1000-fold that of EII'. Construction of various...

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PMID: 1879421
DOI: 10.1111/j.1432-1033.1991.tb21063.x

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