ExplorEnz: EC 3.1.3.62

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3.1.3.62

Accepted name:

multiple inositol-polyphosphate phosphatase

Reaction:

(1) myo-inositol hexakisphosphate + H₂O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
(2) 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H₂O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate
(3) 1D-myo-inositol 1,2,5,6-tetrakisphosphate + H₂O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate
(4) 1D-myo-inositol 1,2,6-trisphosphate + H₂O = 1D-myo-inositol 1,2-bisphosphate + phosphate
(5) 1D-myo-inositol 1,2-bisphosphate + H₂O = 1D-myo-inositol 2-phosphate + phosphate

Glossary:

myo-inositol hexakisphosphate = phytate
1D-myo-inositol 1,3,4,5,6-pentakisphosphate = Ins(1,3,4,5,6)P₅
1D-myo-inositol 1,3,4,5-tetrakisphosphate = Ins(1,3,4,5)P₄
1D-myo-inositol 1,4,5,6-tetrakisphosphate = Ins(1,4,5,6)P₄
1D-myo-inositol 1,4,5-trisphosphate = Ins(1,4,5)P₃
1D-myo-inositol 2,3-bisphosphate = Ins(2,3)P₂
1D-myo-inositol 2-phosphate = Ins(2)P

Other name(s):

MIPP; phytase (ambiguous); 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase (incorrect)

Systematic name:

myo-inositol-hexakisphosphate phosphohydrolase

Comments:

This ubiquitous enzyme degrades myo-inositol hexakisphosphate (phytate) to Ins(2,3)P₂ and Ins(2)P. Activities have been characterized in the yeast Saccharomyces cerevisiae [2], the plant Lupinus albus [3] and the bacteria Bacillus sp. [4] and Raoultella terrigena [5]. In mammal cells Ins(2,3)P₂ and Ins(2)P are the major inositol phosphate compounds found [6]. The mammal enzyme is also active on Ins(1,3,4,5,6)P₅ that is dephosphorylated to Ins(1,4,5,6)P₄ and Ins(1,4,5)P₃, and on 2,3-bisphospho-D-glycerate (cf. EC 3.1.3.80, 2,3-bisphosphoglycerate 3-phosphatase). In addition, it acts on Ins(1,3,4,5)P₄ to yield Ins(1,4,5)P₃ in vitro (cf. EC 3.1.3.67, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase) [7]. It does not hydrolyse phosphates from the 2-positions of inositol phosphates [6]. In other organisms the degradation of phytate follows different routes. (cf. EC 3.1.3.8, 3-phytase, EC 3.1.3.26, 4-phytase, and EC 3.1.3.72, 5-phytase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 116958-30-6

References:

1.	Craxton, A., Caffrey, J.J., Burkhart, W., Safrany, S.T. and Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328 (1997) 75–81. [DOI] [PMID: 9359836]
2.	Greiner, R., Alminger, M.L. and Carlsson, N.G. Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of baker’s yeast. J. Agric. Food Chem. 49 (2001) 2228–2233. [DOI] [PMID: 11368581]
3.	Greiner, R., Larsson Alminger, M., Carlsson, N.G., Muzquiz, M., Burbano, C., Cuadrado, C., Pedrosa, M.M. and Goyoaga, C. Pathway of dephosphorylation of myo-inositol hexakisphosphate by phytases of legume seeds. J. Agric. Food Chem. 50 (2002) 6865–6870. [DOI] [PMID: 12405789]
4.	Greiner, R., Farouk, A., Alminger, M.L. and Carlsson, N.G. The pathway of dephosphorylation of myo-inositol hexakisphosphate by phytate-degrading enzymes of different Bacillus spp. Can. J. Microbiol. 48 (2002) 986–994. [DOI] [PMID: 12556126]
5.	Greiner, R. and Carlsson, N.G. myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena on phytate. Can. J. Microbiol. 52 (2006) 759–768. [DOI] [PMID: 16917535]
6.	Nguyen Trung, M., Kieninger, S., Fandi, Z., Qiu, D., Liu, G., Mehendale, N.K., Saiardi, A., Jessen, H., Keller, B. and Fiedler, D. Stable isotopomers of myo-inositol uncover a complex MINPP1-dependent inositol phosphate network. ACS Cent. Sci. 8 (2022) 1683–1694. [DOI] [PMID: 36589890]
7.	Yu, J., Leibiger, B., Yang, S.N., Shears, S.B., Leibiger, I.B., Berggren, P.O. and Barker, C.J. Multiple inositol polyphosphate phosphatase compartmentalization separates inositol phosphate metabolism from inositol lipid signaling. Biomolecules 13 (2023) . [DOI] [PMID: 37371464]

[EC 3.1.3.62 created 1992, modified 2002, modified 2023]