Format

Send to

Choose Destination
See comment in PubMed Commons below
Appl Microbiol Biotechnol. 2004 Jul;65(1):110-8. Epub 2004 Jan 16.

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

Author information

  • 1Department of Bacterial Genetics, Institute of Biology, Humboldt University, Chaussee-Strasse 117, 10115 Berlin, Germany.

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.

PMID:
14727093
DOI:
10.1007/s00253-003-1530-1
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center