Literature summary for 3.1.3.8 extracted from

Shivange, A.V.; Schwaneberg, U.; Roccatano, D.
Conformational dynamics of active site loop in Escherichia coli phytase (2010), Biopolymers, 93, 994-1002.

Search for more literature for 3.1.3.8

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of crystal structure of the phytate complex of Escherichia coli phytase at pH 6.6 with phytate bound via its 3-phosphate to the active site with Hg2+ as intermolecular bridge, X-ray diffraction structure at 2.28 A resolution, analysis of active site loops, overview	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
myo-inositol hexakis phosphohydrolase	-	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	release of phosphate by stepwise hydrolysis of phosphomonoester bonds in phytate. Phytate is the major storage form of phosphate and inositol, predominantly occurring in cereal grains, legumes, and oilseeds	Escherichia coli
additional information	conformational dynamics of the active site loop, structure analysis, overview. Molecular dynamic studies indicate that the movement in the active site is mainly confined by the active site loop resulted in wider opening of the loop in absence of phytate, possible role of loop residues as prerequisite for highly active phytases	Escherichia coli

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Release 2023.1 (January 2023)