Jump to Main Content
- Fütterer, Ole, et al. Show all 3 Authors
- Applied and environmental microbiology 2006 v.72 no.3 pp. 2206-2211
- EDTA (chelating agent); Escherichia coli; Thermotoga maritima; adenosine triphosphate; amino acid sequences; bacteria; dithiothreitol; enzyme activity; enzymes; genes; hydrolysis; nucleotide sequences; pH; proteins
- ... The gene for a novel [alpha]-amylase, designated AmyC, from the hyperthermophilic bacterium Thermotoga maritima was cloned and heterologously overexpressed in Escherichia coli. The putative intracellular enzyme had no amino acid sequence similarity to glycoside hydrolase family (GHF) 13 [alpha]-amylases, yet the range of substrate hydrolysis and the product profile clearly define the protein as an ...
- PubMed Central: