Abstract
The amino acid sequence of a peptide containing an active serine was examined with poly(3-hydroxybutyrate) (PHB) depolymerase ofAlcaligenes faecalis T1. The sequence Cys-Asn-Ala-Trp-Ala-Gly-Ser-Asn-Ala-Gly-Lys was obtained. This amino acid sequence around the active serine does not fit any reported sequence of other esterases and proteases. On the other hand, a segment of the amino acid sequence of PHB depolymerase ofA. faecalis was homologous to the type III sequence of fibronectin. Similar sequences have been reported in some type of bacterial chitinase and cellulases, and PHB depolymerase seems to have an overall similarity to these bacterial extracellular hydrolases.
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Saito, T., Iwata, A. & Watanabe, T. Molecular structure of extracellular poly(3-hydroxybutyrate) depolymerase fromAlcaligenes faecalis T1. J Environ Polym Degr 1, 99–105 (1993). https://doi.org/10.1007/BF01418202
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DOI: https://doi.org/10.1007/BF01418202