Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa.
AUTOR(ES)
Takekawa, S
RESUMO
The genes for extracellular neutral protease (Npr) and intracellular serine protease (Isp) were cloned from Bacillus polymyxa in order to elucidate the process involved in the generation of multiple beta-amylases and an alpha-amylase from a large amylase precursor. The npr gene was composed of 1,770 bp and 570 amino acids, while the isp gene was composed of 978 bp and 326 amino acids. Both proteases produced by E. coli cleaved the amylase precursor to generate beta- and alpha-amylases. Furthermore, several other proteases produced the same products from the precursor. A 130-kDa amylase precursor has two large domain structures responsible for the generation of beta- and alpha-amylases. The junction region of approximately 200 amino acids may be exposed on the surface of the molecule and susceptible to proteolytic enzymes, which results in the formation of multiple amylases.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=209033Documentos Relacionados
- A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa.
- Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis.
- Cloning and characterization of the beta-amylase gene from Bacillus polymyxa.
- Measurement of microbial alpha-amylases with p-nitrophenyl glycosides as the substrate complex.
- Mutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases.
