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- Publisher
- Springer Journals
- Copyright
- Copyright © 2004 by Springer-Verlag
- Subject
- LifeSciences
- ISSN
- 0175-7598
- eISSN
- 1432-0614
- DOI
- 10.1007/s00253-003-1530-1
- pmid
- 14727093
- Publisher site
- See Article on Publisher Site
Abstract
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.
Journal
Applied Microbiology and Biotechnology – Springer Journals
Published: Jan 16, 2004