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PMID: 14586576 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Biochemical properties and substrate specificities of alkaline and histidine acid phytases.

Applied microbiology and biotechnology ·Vol. 63 ·No. 4 ·2004-01-00 ·Pages 362-72

Oh BC, Choi WC, Park S, Kim YO, Oh TK

Abstract

Phytases are a special class of phosphatase that catalyze the sequential hydrolysis of phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. Phytases are added to animal feedstuff to reduce phosphate pollution in the environment, since monogastric animals such as pigs, poultry, and fish are unable to metabolize phytate. Based on biochemical properties and amino acid sequence alignment, phytases can be categorized into two major classes, the histidine acid phytases and the alkaline phytases. The histidine acid phosphatase class shows broad substrate specificity and hydrolyzes metal-free phytate at the acidic pH range and produces myo-inositol monophosphate as the final product. In contrast, the alkaline phytase class exhibits strict substrate specificity for the calcium-phytate complex and produces myo-inositol trisphosphate as the final product. This review describes recent findings that present novel viewpoints concerning the molecular basis of phytase classification.

MeSH Terms
6-Phytase/chemistry,classification,genetics,metabolism Enzyme Stability Histidine Hydrogen-Ion Concentration Hydrolysis Models, Molecular Phylogeny Phytic Acid/metabolism Substrate Specificity
Chemicals
Histidine Phytic Acid 6-Phytase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Oh B-C
Microbial Genomics Laboratory, Korea Research Institute of Bioscience and Biotechnology, P.O. Box 115, 305-600 Yusong, Taejon, Korea.
Choi W-C
Park S
Kim Y-o
Oh T-K
Article Info
Journal
Applied microbiology and biotechnology
Abbr.
Appl Microbiol Biotechnol
ISSN
0175-7598
Published
2004-01-00
Epub
2003-00-28
Pages
362-72
Language
English
Region
Germany
NLM ID
8406612
Subset
IM
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