EzCatDB: T00053

DB codeT00053
RLCP classification1.15.7910.1164
CATH domainDomain 14.10.460.10
Domain 23.30.540.10Catalytic domain
Domain 33.40.190.80Catalytic domain
E.C.3.1.3.57
CSA1inp

CATH domainRelated DB codes (homologues)
3.30.540.10D00148,D00153,D00491
3.40.190.80D00148,D00153,D00491

Enzyme Name
Swiss-protKEGG

P21327
Protein nameInositol polyphosphate 1-phosphataseinositol-1,4-bisphosphate 1-phosphatase
inositol-polyphosphate 1-phosphatase
SynonymsIPPase
IPP
EC 3.1.3.57

KEGG pathways
MAP codePathways
MAP00562Inositol phosphate metabolism
MAP04070Phosphatidylinositol signaling system

Swiss-prot:Accession NumberP21327
Entry nameINPP_BOVIN
Activity1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate.
SubunitMonomer.
Subcellular location
CofactorMagnesium.


CofactorsSubstratesProducts
KEGG-idC00305C01220C00001C01243C03546C00009C04063
CompoundMagnesiumD-myo-Inositol 1,4-bisphosphateH2O1D-myo-Inositol 1,3,4-trisphosphateD-myo-Inositol 4-phosphateOrthophosphateD-myo-Inositol 3,4-bisphosphate
Typedivalent metal (Ca2+, Mg2+)carbohydrate,phosphate group/phosphate ionH2Ocarbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ionphosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ion
1inpA01UnboundUnbound
UnboundUnboundUnboundUnbound
1inpA02Bound:2x_MGUnbound
UnboundUnboundUnboundUnbound
1inpA03UnboundUnbound
UnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1inp & Swiss-prot;P21327 & literature [2], [7]
pdbCatalytic residuesCofactor-binding residues
1inpA01

1inpA02ASP 54;THR 158
ASP 153;ASP 156(Magnesium-1 binding);GLU 79;ASP 153;ILE 155(Magnesium-2 binding)
1inpA03
ASP 317(Magnesium-1 binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]

[3]

[7]Fig.5, p.683

references
[1]
PubMed ID2537096
JournalBiochim Biophys Acta
Year1989
Volume1001
Pages134-44
AuthorsHansen CA, Inubushi T, Williamson MT, Williamson JR
TitlePartial purification of inositol polyphosphate 1-phosphomonoesterase with characterization of its substrates and products by nuclear magnetic resonance spectroscopy.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID95034747
PubMed ID7947723
JournalBiochemistry
Year1994
Volume33
Pages13164-71
AuthorsYork JD, Ponder JW, Chen ZW, Mathews FS, Majerus PW
TitleCrystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution.
Related PDB1inp
Related Swiss-protP21327
[3]
PubMed ID7946962
JournalCell Signal
Year1994
Volume6
Pages355-62
AuthorsLuttrell BM
TitleCellular actions of inositol phosphates and other natural calcium and magnesium chelators.
[4]
PubMed ID8107142
JournalJ Mol Biol
Year1994
Volume236
Pages584-9
AuthorsYork JD, Chen ZW, Ponder JW, Chauhan AK, Mathews FS, Majerus PW
TitleCrystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells.
[5]
PubMed ID7761465
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages5149-53
AuthorsYork JD, Ponder JW, Majerus PW
TitleDefinition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure.
[6]
PubMed ID9762363
JournalAdv Enzyme Regul
Year1998
Volume38
Pages365-74
AuthorsYork JD, Xiong JP, Spiegelberg B
TitleNuclear inositol signaling: a structural and functional approach.
[7]
PubMed ID11812139
JournalJ Mol Biol
Year2002
Volume315
Pages677-85
AuthorsPatel S, Yenush L, Rodriguez PL, Serrano R, Blundell TL
TitleCrystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a novel target of lithium therapy.

comments
This enzyme is homologous to PIPase(DB code;D00491) with a similar active site, suggesting that it has a similar mechanism to that of the homologous enzyme.

createdupdated
2005-09-062009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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