Inositol-polyphosphate 5-phosphatase

The enzyme inositol-polyphosphate 5-phosphatase (EC 3.1.3.56), systematic name 1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase, catalyses the following reactions:

(1) D-myo-inositol 1,4,5-trisphosphate + H₂O

\rightleftharpoons

myo-inositol 1,4-bisphosphate + phosphate

(2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H₂O

\rightleftharpoons

1D-myo-inositol 1,3,4-trisphosphate + phosphate

Ten mammalian isoforms are known.

Other names of this enzyme include type I inositol-polyphosphate phosphatase, inositol trisphosphate phosphomonoesterase, InsP₃/Ins(1,3,4,5)P₄ 5-phosphatase, inosine triphosphatase, D-myo-inositol 1,4,5-triphosphate 5-phosphatase, D-myo-inositol 1,4,5-trisphosphate 5-phosphatase, L-myo-inositol 1,4,5-trisphosphate-monoesterase, inositol phosphate 5-phosphomonoesterase, inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase, Ins(1,4,5)P₃ 5-phosphataseD-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase, inositol 1,4,5-trisphosphate phosphatase, inositol polyphosphate-5-phosphatase, myo-inositol-1,4,5-trisphosphate 5-phosphatase, inositol-1,4,5-trisphosphate 5-phosphatase.

References

Ooms LM, Horan KA, Rahman P, Seaton G, Gurung R, Kethesparan DS, Mitchell CA (2009). "The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease". The Biochemical Journal. 419 ( Pt 1): 29–49. doi:10.1042/BJ20081673. PMID 19272022.
Downes CP, Mussat MC, Michell RH (April 1982). "The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane". The Biochemical Journal. 203 (1): 169–77. doi:10.1042/bj2030169. PMC 1158207. PMID 6285891.
Erneux C, Lemos M, Verjans B, Vanderhaeghen P, Delvaux A, Dumont JE (May 1989). "Soluble and particulate Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase in bovine brain". European Journal of Biochemistry. 181 (2): 317–22. doi:10.1111/j.1432-1033.1989.tb14726.x. PMID 2540972.
Woscholski, R.; Parker, P.J. (2000). "Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates". In Cockcroft, S. (ed.). Biology of Phosphoinositides. Oxford: Biology of Phosphoinositides. pp. 320–338.
Verjans B, De Smedt F, Lecocq R, Vanweyenberg V, Moreau C, Erneux C (May 1994). "Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase". The Biochemical Journal. 300 ( Pt 1): 85–90. doi:10.1042/bj3000085. PMC 1138127. PMID 8198557.

External links

Inositol-polyphosphate+5-phosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.1.3