Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1

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Item Type:	Article
Title:	Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1
Creators Name:	Sajidan, A., Farouk, A., Greiner, R., Jungblut, P., Mueller, E.C. and Borriss, R.
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 myoinositol 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.
Keywords:	Klebsiella, Phosphoric Monoester Hydrolases, Phylogeny, Phytic Acid, Soil Microbiology
Source:	Applied Microbiology and Biotechnology
ISSN:	0175-7598
Publisher:	Springer
Volume:	65
Number:	1
Page Range:	110-118
Date:	1 January 2004
Official Publication:	https://doi.org/10.1007/s00253-003-1530-1
PubMed:	View item in PubMed

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