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....
Topics
- Amidohydrolases
- Amino Acid Sequence
- Amino Acids
- Base Sequence
- Enzyme Activation
- Escherichia coli
- Flavobacterium
- Molecular Sequence Data
- Mutation
- Oligonucleotides
- Open Reading Frames
- Plasmids
- Sequence Homology, Nucleic Acid
- Structure-Activity Relationship
- Substrate Specificity