Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate

Zeng, Yi‐Fang; Ko, Tzu‐Ping; Lai, H.L.; Cheng, Ya‐Shan; Wu, Tzu-Hui; Ma, Yanhe; Chen, Chun‐Chi; Yang, Chii-Shen; Cheng, K.-J.; Huang, Chun‐Hsiang; Guo, Rey‐Ting; Liu, Je-Ruei

doi:10.1016/j.jmb.2011.03.063

Cited by 35 publications

(22 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similar to the phytases previously characterized from Bacillus species [29,[31][32][33], the PHY US573 showed dependence toward calcium for its catalytic activity. Increasing the concentration of this metal ion enhanced the enzyme activity, which attains its maximal level in the presence of 1 mM CaCl 2 .…”

Section: Calcium Requirement For Phy Us573 Activitysupporting

confidence: 62%

“…Indeed, the residue V346 is present in PHY US573 in a loop near the calcium ions binding sites (high affinity). These calcium Ca1 and Ca2 are involved in the thermal stability [33,34]. The presence of V instead of the A in this position could reduce the flexibility of the loop (by decreasing the effect of the side chain in the thermal agitation) and therefore, improves the thermal stability of the enzyme especially at high temperatures as observed in the case of PHY US573 (Fig.…”

Section: Cloning and Structural Analysis Of Phy Us573mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of an extremely salt-tolerant and thermostable phytase from Bacillus amyloliquefaciens US573

Boukhris

Farhat-Khemakhem

Blibech

et al. 2015

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Section: Calcium Requirement For Phy Us573 Activitysupporting

confidence: 62%

Section: Cloning and Structural Analysis Of Phy Us573mentioning

confidence: 99%

Characterization of an extremely salt-tolerant and thermostable phytase from Bacillus amyloliquefaciens US573

Boukhris

Farhat-Khemakhem

Blibech

et al. 2015

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…The enzyme was found to be more thermostable in presence of Ca 2+ ions, indicating the stabilizing effect of the ion on the enzyme against thermal denaturation. Previous studies have already reported alkaline phytases being highly specific for the calcium‐phytate complex and require Ca 2+ ion for activity . In fact, Bacillus phytases required calcium for their active conformation and hence, loss of enzymatic activity occurred in calcium‐depleted conditions due to a conformational change .…”

Section: Discussionmentioning

confidence: 99%

A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

Roy

Datta

Ghosh

2017

Biotechnology Progress

View full text Add to dashboard Cite

Bacillus aryabhattai RS1 isolated from rhizosphere produced an extracellular, low temperature active phytase. The cultural conditions for enzyme production were optimized to obtain 35 U mL of activity. Purified phytase had specific activity and molecular weight of 72.97 U mg and ∼40 kDa, respectively. The enzyme was optimally active at pH 6.5 and 40°C and was highly specific to phytate. It exhibited higher catalytic activity at low temperature, retaining over 40% activity at 10°C. Phytase was more thermostable in presence of Ca ion and retained 100% residual activity on preincubation at 20-50°C for 30 min. Partial phytase encoding gene, phy (816 bp) was cloned and sequenced. The encoded amino acid sequence (272 aa) contained two conserved motifs, DA[A/T/E]DDPA[I/L/V]W and NN[V/I]D[I/L/V]R[Y/D/Q] of β-propellar phytase and had lower sequence homology with other Bacillus phytases, indicating its novelty. Phytase and the bacterial inoculum were effective in improving germination and growth of chickpea seedlings under phosphate limiting condition. Moreover, the potential applications of the enzyme with relatively high activity at lower temperatures (20-30°C) could also be extended to aquaculture and food processing. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:633-641, 2017.

show abstract

“…Structures of phytate or phytate-analogue complexes have been reported with either the 3- or 5-phosphate group in the catalytic centre. For the 3-position these are Ec Phy [22] (PDB code 1dkq) and An Phy [24] (PDB 3k4q) from the HAPP family, and a B. subtilis β-propeller phytase [33] (PDB 3ams, 3amr); while for the 5-position there is a S. ruminantium cysteine phytase [31] (PDB 1u26).…”

Section: Introductionmentioning

confidence: 99%

Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution Study

et al. 2013

View full text Add to dashboard Cite

Phytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), β-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site.

show abstract

Crystal Structures of Bacillus Alkaline Phytase in Complex with Divalent Metal ions and Inositol Hexasulfate

Cited by 35 publications

References 28 publications

Characterization of an extremely salt-tolerant and thermostable phytase from Bacillus amyloliquefaciens US573

Characterization of an extremely salt-tolerant and thermostable phytase from Bacillus amyloliquefaciens US573

A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution Study

Contact Info

Product

Resources

About