Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.26 extracted from

  • Pal Roy, M.; Mazumdar, D.; Dutta, S.; Saha, S.P.; Ghosh, S.
    Cloning and expression of phytase appA gene from Shigella sp. CD2 in Pichia pastoris and comparison of properties with recombinant enzyme expressed in E. coli (2016), PLoS ONE, 11, e0145745 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene appA or phyS, cloning from library, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of extracellular His-tagged enzyme in Escherichia coli strain BL21(DE3) as nonglycosylated protein and of extracellular nontagged enzyme in Pichia pastoris strain GS115(his4) under control of the AOX1 promoter as glycosylated protein Shigella sp. CD2

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Shigella sp. CD2
EDTA
-
Shigella sp. CD2
Fe2+
-
Shigella sp. CD2
additional information the recombinant enzyme shows resistance to trypsin Shigella sp. CD2
Zn2+
-
Shigella sp. CD2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli Shigella sp. CD2
0.22
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris Shigella sp. CD2

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Shigella sp. CD2
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Shigella sp. CD2
Mg2+ activates Shigella sp. CD2
Mn2+ activates Shigella sp. CD2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol hexakisphosphate + H2O Shigella sp. CD2 phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72 1D-myo-inositol pentakisphosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Shigella sp. CD2 F6IQ86 isolated from wheat rhizosphere
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein enzyme AppAS contains three potential sites of N-glycosylation, recombinant nontagged enzyme from Pichia pastoris strain GS115(his4) is glycosylated, deglycosylation of rAppAP is carried out using Endo H deglycosylase Shigella sp. CD2

Purification (Commentary)

Purification (Comment) Organism
recombinant nonglycosylated His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant glycosylated nontagged enzyme from Pichia pastoris strain GS115(his4) by cation exchange chromatography Shigella sp. CD2

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
967
-
purified recombinant glycosylated enzyme expressed from Pichia pastoris, pH 5.5, 37°C Shigella sp. CD2
2982
-
purified recombinant nonglycosylated enzyme expressed from Escherichia coli, pH 5.5, 37°C Shigella sp. CD2

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme shows no or poor activity with ATP, ADP, 4-nitrophenyl phosphate, diphosphate, glucose 6-phosphate, and fructose 6-phosphate Shigella sp. CD2 ?
-
?
myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8, 3.1.3.26, and 3.1.3.72 Shigella sp. CD2 1D-myo-inositol pentakisphosphate + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 59000-65000, recombinant glycosylated enzyme from Pichia pastoris, SDS-PAGE, x * 45000, recombinant deglycosylated enzyme from Pichia pastoris, SDS-PAGE Shigella sp. CD2
More AppAS contains three potential sites of N-glycosylation, a putative signal peptide of 22 amino acids at N-terminal end and 8 cysteine residues among which 99-130, 200-210, 404-413 are the most possible disulfide bond pairs. The calculated molecular mass of the protein with and without the signal sequence are about 47 and 45 kDa, respectively Shigella sp. CD2

Synonyms

Synonyms Comment Organism
AppA
-
Shigella sp. CD2
AppAS
-
Shigella sp. CD2
More cf. EC 3.1.3.8 and 3.1.3.72 Shigella sp. CD2
phyS
-
Shigella sp. CD2
phytase
-
Shigella sp. CD2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
recombinant enzyme Shigella sp. CD2

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 80 and below, activity profile overview, recombinant enzymes Shigella sp. CD2

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
720
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris Shigella sp. CD2
2230
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli Shigella sp. CD2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
recombinant enzyme Shigella sp. CD2

pH Range

pH Minimum pH Maximum Comment Organism
2.5 8.5 activity range, profile overview, over 50% of activity at pH 3.5-6.5 Shigella sp. CD2

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3272.7
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris Shigella sp. CD2
12389
-
myo-inositol hexakisphosphate pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli Shigella sp. CD2