Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1
| Autor: | Rainer Borriss, E.-C. Müller, A. Sajidan, P. Jungblut, Ralf Greiner, A. Farouk |
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| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
Sugar phosphates Phytic Acid Phosphatase General Medicine Biology medicine.disease_cause Applied Microbiology and Biotechnology Phosphoric Monoester Hydrolases Gene product Enzyme chemistry Biochemistry Klebsiella medicine Phytase Escherichia coli Peptide sequence Histidine Phylogeny Soil Microbiology Biotechnology |
| Zdroj: | Applied microbiology and biotechnology. 65(1) |
| ISSN: | 0175-7598 |
| Popis: | Klebsiella sp. strain ASR1 isolated from an Indonesian rice field is able to hydrolyse myo-inositol hexakis phosphate (phytate). The phytase protein was purified and characterised as a 42 kDa protein accepting phytate, NADP and sugar phosphates as substrates. The corresponding gene (phyK) was cloned from chromosomal DNA using a combined approach of protein and genome analysis, and expressed in Escherichia coli. The recombinant enzyme was identified as a 3-phytase yielding myo-inositol monophosphate, Ins(2)P, as the final product of enzymatic phytate hydrolysis. Based on its amino acid sequence, PhyK appears to be a member of a hitherto unknown subfamily of histidine acid phytate-degrading enzymes with the active site RHGXRXP and HD sequence motifs, and is different from other general phosphatases and phytases. Due to its ability to degrade sodium phytate to the mono phosphate ester, the phyK gene product is an interesting candidate for industrial and agricultural applications to make phytate phosphorous available for plant and animal nutrition. |
| Databáze: | OpenAIRE |
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