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Literature summary for 3.1.3.8 extracted from

  • Tung, E.T.; Ma, H.W.; Cheng, C.; Lim, B.L.; Wong, K.B.
    Stabilization of beta-propeller phytase by introducing Xaa-->Pro and Gly-->Ala substitutions at consensus positions (2008), Protein Pept. Lett., 15, 297-299.
    View publication on PubMed
Search for more literature for 3.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
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 Bacillus licheniformis

Protein Variants

Protein Variants Comment Organism
G117A/G266A mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at G177 and G266 results in a substantial stabilization of PhyL compared to wild-type (DELTAG value of 8 kJ/mol) with an elevated DELTAG value of 20 kJ/mol Bacillus licheniformis
H32P/S256P/K304P/K324P/S353P mutant shows similar Km, kcat and optimal Ca2+-concentration values to wild-type, mutation at 5 consensus positions only slightly enhances stabilization compared to wild-type (DELTAG value of 8 kJ/mol) with a DELTAG value of 8.8 kJ/mol Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
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 the enzyme may be a 3-phytase, EC 3.1.3.8, or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate (3-phytase) or 1D-myo-inositol 1,2,3,5,6-pentakisphosphate (4-phytase) (i.e. 1L-myo-inositol 1,2,3,4,5-pentakisphosphate if 1L numbering is applied) has not been analyzed. The reaction was monitored by analyzing the released phosphate
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Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus licheniformis

Synonyms

Synonyms Comment Organism
phyL
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 Bacillus licheniformis