EzCatDB: D00153

DB codeD00153
RLCP classification1.15.7910.1164
CATH domainDomain 13.30.540.10Catalytic domain
Domain 23.40.190.80Catalytic domain
E.C.3.1.3.25
CSA1ima

CATH domainRelated DB codes (homologues)
3.30.540.10D00148,D00491,T00053
3.40.190.80D00148,D00491,T00053

Enzyme Name
Swiss-protKEGG

Q57573O30298P20456P29218
Protein nameInositol-1-monophosphataseInositol-1-monophosphataseInositol monophosphataseInositol monophosphataseinositol-phosphate phosphatase
myo-inositol-1(or 4)-monophosphatase
inositol 1-phosphatase
L-myo-inositol-1-phosphate phosphatase
myo-inositol 1-phosphatase
inositol phosphatase
inositol monophosphate phosphatase
inositol-1(or 4)-monophosphatase
myo-inositol-1(or 4)-phosphate phosphohydrolase
myo-inositol monophosphatase
myo-inositol-1-phosphatase
SynonymsIMPase
Inositol-1-phosphatase
I-1-Pase
EC 3.1.3.25
IMPase
Inositol-1-phosphatase
I-1-Pase
EC 3.1.3.25
EC 3.1.3.25
Inositol-1(or 4)-monophosphatase
IMPase
IMP
Lithium-sensitive myo-inositol monophosphatase A1
EC 3.1.3.25
Inositol-1(or 4)-monophosphatase
IMPase
IMP
Lithium-sensitive myo-inositol monophosphatase A1

KEGG pathways
MAP codePathways
MAP00521Streptomycin biosynthesis
MAP00562Inositol phosphate metabolism
MAP04070Phosphatidylinositol signaling system

Swiss-prot:Accession NumberQ57573O30298P20456P29218
Entry nameSUHB_METJASUHB_ARCFUIMPA1_BOVINIMPA1_HUMAN
ActivityMyo-inositol phosphate + H(2)O = myo-inositol + phosphate.Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.Myo-inositol phosphate + H(2)O = myo-inositol + phosphate.
SubunitHomodimer.
Homodimer.Homodimer.
Subcellular location

Cytoplasm.Cytoplasm.
CofactorMagnesium.Magnesium (By similarity).Magnesium.Magnesium.


CofactorsSubstratesProducts
KEGG-idC00305C01177C03546C00001C00137C00009
CompoundMagnesium1L-myo-Inositol 1-phosphatemyo-Inositol 4-phosphateH2Omyo-InositolOrthophosphate
Typedivalent metal (Ca2+, Mg2+)carbohydrate,phosphate group/phosphate ioncarbohydrate,phosphate group/phosphate ionH2Ocarbohydratephosphate group/phosphate ion
1dk4A01Analogue:3x_ZNUnboundUnbound
UnboundBound:PO4
1dk4B01Analogue:3x_ZNUnboundUnbound
UnboundBound:PO4
1g0hA01Analogue:2x_CABound:IPDUnbound
UnboundUnbound
1g0hB01Analogue:2x_CABound:IPDUnbound
UnboundUnbound
1g0iA01Analogue:3x_MNUnboundUnbound
UnboundBound:PO4
1g0iB01Analogue:3x_MNUnboundUnbound
UnboundBound:PO4
1lbvA01UnboundUnboundUnbound
UnboundUnbound
1lbvB01UnboundUnboundUnbound
UnboundUnbound
1lbwA01UnboundUnboundUnbound
UnboundUnbound
1lbwB01UnboundUnboundUnbound
UnboundUnbound
1lbxA01Analogue:2x_CABound:IPDUnbound
UnboundUnbound
1lbxB01Analogue:2x_CABound:IPDUnbound
UnboundUnbound
1lbyA01Analogue:3x_MNUnboundUnbound
UnboundBound:PO4
1lbyB01Analogue:3x_MNUnboundUnbound
UnboundBound:PO4
1lbzA01Analogue:3x_CAAnalogue:FBPUnbound
UnboundUnbound
1lbzB01Analogue:3x_CAAnalogue:FBPUnbound
UnboundUnbound
2bjiA01Bound:3x_MGUnboundUnbound
UnboundUnbound
2bjiB01Bound:3x_MGUnboundUnbound
UnboundUnbound
1awbA01Analogue:3x_CABound:IPDUnbound
UnboundUnbound
1awbB01Analogue:3x_CABound:IPDUnbound
UnboundUnbound
1imaA01Analogue:_GDBound:IPDUnbound
UnboundUnbound
1imaB01Analogue:_GDBound:IPDUnbound
UnboundUnbound
1imbA01Analogue:_GDBound:LIPUnbound
UnboundUnbound
1imbB01Analogue:_GDBound:LIPUnbound
UnboundUnbound
1imcA01Analogue:3x_MNUnboundUnbound
UnboundUnbound
1imcB01Analogue:3x_MNUnboundUnbound
UnboundUnbound
1imdA01Analogue:2x_MNUnboundUnbound
UnboundBound:PO4
1imdB01Analogue:2x_MNUnboundUnbound
UnboundBound:PO4
1imeA01Analogue:_CAUnboundUnbound
UnboundUnbound
1imeB01Analogue:_CAUnboundUnbound
UnboundUnbound
1imfA01UnboundUnboundUnbound
UnboundUnbound
2hhmA01Analogue:_GDUnboundUnbound
UnboundAnalogue:SO4
2hhmB01Analogue:_GDUnboundUnbound
UnboundAnalogue:SO4
1dk4A02UnboundUnboundUnbound
UnboundUnbound
1dk4B02UnboundUnboundUnbound
UnboundUnbound
1g0hA02UnboundUnboundUnbound
UnboundUnbound
1g0hB02UnboundUnboundUnbound
UnboundUnbound
1g0iA02UnboundUnboundUnbound
Bound:INSUnbound
1g0iB02UnboundUnboundUnbound
Bound:INSUnbound
1lbvA02UnboundUnboundUnbound
UnboundUnbound
1lbvB02UnboundUnboundUnbound
UnboundUnbound
1lbwA02UnboundUnboundUnbound
UnboundUnbound
1lbwB02UnboundUnboundUnbound
UnboundUnbound
1lbxA02UnboundUnboundUnbound
UnboundUnbound
1lbxB02UnboundUnboundUnbound
UnboundUnbound
1lbyA02UnboundUnboundUnbound
Analogue:F6PUnbound
1lbyB02UnboundUnboundUnbound
Analogue:F6PUnbound
1lbzA02UnboundUnboundUnbound
UnboundUnbound
1lbzB02UnboundUnboundUnbound
UnboundUnbound
2bjiA02UnboundUnboundUnbound
UnboundUnbound
2bjiB02UnboundUnboundUnbound
UnboundUnbound
1awbA02UnboundUnboundUnbound
UnboundUnbound
1awbB02UnboundUnboundUnbound
UnboundUnbound
1imaA02UnboundUnboundUnbound
UnboundUnbound
1imaB02UnboundUnboundUnbound
UnboundUnbound
1imbA02UnboundUnboundUnbound
UnboundUnbound
1imbB02UnboundUnboundUnbound
UnboundUnbound
1imcA02UnboundUnboundUnbound
UnboundUnbound
1imcB02UnboundUnboundUnbound
UnboundUnbound
1imdA02UnboundUnboundUnbound
UnboundUnbound
1imdB02UnboundUnboundUnbound
UnboundUnbound
1imeA02UnboundUnboundUnbound
UnboundUnbound
1imeB02UnboundUnboundUnbound
UnboundUnbound
1imfA02UnboundUnboundUnbound
UnboundUnbound
2hhmA02UnboundUnboundUnbound
UnboundUnbound
2hhmB02UnboundUnboundUnbound
UnboundUnbound

Active-site residues
resource
Swiss-prot;P29218, O30298, Q57573 & Literature [8], [20], [23], [27], [28]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
1dk4A01ASP   44;SER   86
GLU   65(Magnesium-1 & -3);ASP   81(Magnesium-1 & -2);ASP   84(Magnesium-2);ILE   83(Magnesium-1);ASP   38;        (Magnesium-3)
GLY   85;SER   86
1dk4B01ASP  344;SER  386
GLU  365(Magnesium-1 & -3);ASP  381(Magnesium-1 & -2);ASP  384(Magnesium-2);ILE  383(Magnesium-1);ASP  338;        (Magnesium-3)
GLY  385;SER  386
1g0hA01ASP   44;SER   86
GLU   65(Magnesium-1 & -3);ASP   81(Magnesium-1 & -2);ASP   84(Magnesium-2);ILE   83(Magnesium-1);ASP   38;        (Magnesium-3)
GLY   85;SER   86
1g0hB01ASP  344;SER  386
GLU  365(Magnesium-1 & -3);ASP  381(Magnesium-1 & -2);ASP  384(Magnesium-2);ILE  383(Magnesium-1);ASP  338;        (Magnesium-3)
GLY  385;SER  386
1g0iA01ASP   44;SER   86
GLU   65(Magnesium-1 & -3);ASP   81(Magnesium-1 & -2);ASP   84(Magnesium-2);ILE   83(Magnesium-1);ASP   38;        (Magnesium-3)
GLY   85;SER   86
1g0iB01ASP  344;SER  386
GLU  365(Magnesium-1 & -3);ASP  381(Magnesium-1 & -2);ASP  384(Magnesium-2);ILE  383(Magnesium-1);ASP  338;        (Magnesium-3)
GLY  385;SER  386
1lbvA01ASP   46;THR   87
GLU   67(Magnesium-1 & -3);ASP   82(Magnesium-1 & -2);ASP   85(Magnesium-2);LEU   84(Magnesium-1);ASP   38;THR   40(Magnesium-3)
GLY   86;THR   87
1lbvB01ASP  346;THR  387
GLU  367(Magnesium-1 & -3);ASP  382(Magnesium-1 & -2);ASP  385(Magnesium-2);LEU  384(Magnesium-1);ASP  338;THR  340(Magnesium-3)
GLY  386;THR  387
1lbwA01ASP   46;THR   87
GLU   67(Magnesium-1 & -3);ASP   82(Magnesium-1 & -2);ASP   85(Magnesium-2);LEU   84(Magnesium-1);ASP   38;THR   40(Magnesium-3)
GLY   86;THR   87
1lbwB01ASP  346;THR  387
GLU  367(Magnesium-1 & -3);ASP  382(Magnesium-1 & -2);ASP  385(Magnesium-2);LEU  384(Magnesium-1);ASP  338;THR  340(Magnesium-3)
GLY  386;THR  387
1lbxA01ASP   46;THR   87
GLU   67(Magnesium-1 & -3);ASP   82(Magnesium-1 & -2);ASP   85(Magnesium-2);LEU   84(Magnesium-1);ASP   38;THR   40(Magnesium-3)
GLY   86;THR   87
1lbxB01ASP  346;THR  387
GLU  367(Magnesium-1 & -3);ASP  382(Magnesium-1 & -2);ASP  385(Magnesium-2);LEU  384(Magnesium-1);ASP  338;THR  340(Magnesium-3)
GLY  386;THR  387
1lbyA01ASP   46;THR   87
GLU   67(Magnesium-1 & -3);ASP   82(Magnesium-1 & -2);ASP   85(Magnesium-2);LEU   84(Magnesium-1);ASP   38;THR   40(Magnesium-3)
GLY   86;THR   87
1lbyB01ASP  346;THR  387
GLU  367(Magnesium-1 & -3);ASP  382(Magnesium-1 & -2);ASP  385(Magnesium-2);LEU  384(Magnesium-1);ASP  338;THR  340(Magnesium-3)
GLY  386;THR  387
1lbzA01ASP   46;THR   87
GLU   67(Magnesium-1 & -3);ASP   82(Magnesium-1 & -2);ASP   85(Magnesium-2);LEU   84(Magnesium-1);ASP   38;THR   40(Magnesium-3)
GLY   86;THR   87
1lbzB01ASP  346;THR  387
GLU  367(Magnesium-1 & -3);ASP  382(Magnesium-1 & -2);ASP  385(Magnesium-2);LEU  384(Magnesium-1);ASP  338;THR  340(Magnesium-3)
GLY  386;THR  387
2bjiA01ASP 1047;THR 1095
GLU 1070(Magnesium-1 & -3);ASP 1090(Magnesium-1 & -2);ASP 1093(Magnesium-2);ILE 1092(Magnesium-1);ASP 1041;        (Magnesium-3)
GLY 1094;THR 1095
2bjiB01ASP 2047;THR 2095
GLU 2070(Magnesium-1 & -3);ASP 2090(Magnesium-1 & -2);ASP 2093(Magnesium-2);ILE 2092(Magnesium-1);ASP 2041;        (Magnesium-3)
GLY 2094;THR 2095
1awbA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1awbB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imaA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imaB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imbA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imbB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imcA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imcB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imdA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imdB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imeA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imeB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1imfA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
2hhmA01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
2hhmB01ASP   47;THR   95
GLU   70(Magnesium-1 & -3);ASP   90(Magnesium-1 & -2);ASP   93(Magnesium-2);ILE   92(Magnesium-1);ASP   41;        (Magnesium-3)
GLY   94;THR   95
1dk4A02
ASP  201(Magnesium-2)

1dk4B02
ASP  501(Magnesium-2)

1g0hA02
ASP  201(Magnesium-2)

1g0hB02
ASP  501(Magnesium-2)

1g0iA02
ASP  201(Magnesium-2)

1g0iB02
ASP  501(Magnesium-2)

1lbvA02
ASP  200(Magnesium-2)

1lbvB02
ASP  500(Magnesium-2)

1lbwA02
ASP  200(Magnesium-2)

1lbwB02
ASP  500(Magnesium-2)

1lbxA02
ASP  200(Magnesium-2)

1lbxB02
ASP  500(Magnesium-2)

1lbyA02
ASP  200(Magnesium-2)

1lbyB02
ASP  500(Magnesium-2)

1lbzA02
ASP  200(Magnesium-2)

1lbzB02
ASP  500(Magnesium-2)

2bjiA02
ASP 1220(Magnesium-2)

2bjiB02
ASP 2220(Magnesium-2)

1awbA02
ASP  220(Magnesium-2)

1awbB02
ASP  220(Magnesium-2)

1imaA02
ASP  220(Magnesium-2)

1imaB02
ASP  220(Magnesium-2)

1imbA02
ASP  220(Magnesium-2)

1imbB02
ASP  220(Magnesium-2)

1imcA02
ASP  220(Magnesium-2)

1imcB02
ASP  220(Magnesium-2)

1imdA02
ASP  220(Magnesium-2)

1imdB02
ASP  220(Magnesium-2)

1imeA02
ASP  220(Magnesium-2)

1imeB02
ASP  220(Magnesium-2)

1imfA02
ASP  220(Magnesium-2)

2hhmA02
ASP  220(Magnesium-2)

2hhmB02
ASP  220(Magnesium-2)


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]p.9474-9475
[8]Fig.5, p.9466
[10]Fig.4, p.5-6
[16]

[20]Fig.2, Fig.5, p.268-269
[27]Fig.5, p.681-682
[28]Fig.5, p.553

references
[1]
PubMed ID1665957
JournalAnal Biochem
Year1991
Volume198
Pages375-8
AuthorsChurchich JE, Kwok F
TitleAssay of 1L-myo-inositol-1-phosphatase using a fluorometric method.
[2]
PubMed ID1333077
JournalPharm Res
Year1992
Volume9
Pages1370-3
AuthorsHarrold MW, Sriburi A, Caimano P, Qi H, Seybert D, Lin FT
TitleInhibition of myo-inositol 1-phosphatase by cis-1,2,3-cyclohexanetriol 1-phosphate, a molecular simplification of the natural substrate.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID93066173
PubMed ID1332026
JournalProc Natl Acad Sci U S A
Year1992
Volume89
Pages10031-5
AuthorsBone R, Springer JP, Atack JR
TitleStructure of inositol monophosphatase, the putative target of lithium therapy.
Related PDB2hhm
Related Swiss-protP29218
[4]
PubMed ID8382485
JournalBiochem Biophys Res Commun
Year1993
Volume190
Pages1080-3
AuthorsZhang Y, Liang JY, Lipscomb WN
TitleStructural similarities between fructose-1,6-bisphosphatase and inositol monophosphatase.
[5]
PubMed ID8223565
JournalEur J Biochem
Year1993
Volume217
Pages281-7
AuthorsPollack SJ, Knowles MR, Atack JR, Broughton HB, Ragan CI, Osborne S, McAllister G
TitleProbing the role of metal ions in the mechanism of inositol monophosphatase by site-directed mutagenesis.
[6]
PubMed ID8019438
JournalBiochem Mol Biol Int
Year1994
Volume32
Pages325-30
AuthorsKwok F, Lo SC, Churchich JE
TitleBrain myo-inositol monophosphatase: activity of the single subunit in a dimeric enzyme.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
PubMed ID8068621
JournalBiochemistry
Year1994
Volume33
Pages9468-76
AuthorsBone R, Frank L, Springer JP, Atack JR
TitleStructural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis.
Related PDB1imc,1imd,1ime,1imf
[8]
CommentsX-ray crystallography
PubMed ID8068620
JournalBiochemistry
Year1994
Volume33
Pages9460-7
AuthorsBone R, Frank L, Springer JP, Pollack SJ, Osborne SA, Atack JR, Knowles MR, McAllister G, Ragan CI, Broughton HB, et al
TitleStructural analysis of inositol monophosphatase complexes with substrates.
Related PDB1ima,1imb
[9]
PubMed ID8276805
JournalJ Biol Chem
Year1994
Volume269
Pages266-71
AuthorsKwon OS, Churchich JE
TitleInteraction of 70-kDA heat shock cognate protein with peptides and myo-inositol monophosphatase.
[10]
PubMed ID7890024
JournalFEBS Lett
Year1995
Volume361
Pages1-7
AuthorsAtack JR, Broughton HB, Pollack SJ
TitleStructure and mechanism of inositol monophosphatase.
[11]
PubMed ID7568043
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages8916-20
AuthorsVilleret V, Huang S, Fromm HJ, Lipscomb WN
TitleCrystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase.
[12]
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.
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, AND MUTAGENESIS OF LYS-36.
PubMed ID8718889
JournalBiochemistry
Year1996
Volume35
Pages10957-66
AuthorsGanzhorn AJ, Lepage P, Pelton PD, Strasser F, Vincendon P, Rondeau JM
TitleThe contribution of lysine-36 to catalysis by human myo-inositol monophosphatase.
Related Swiss-protP29218
[14]
PubMed ID8925839
JournalEur J Biochem
Year1996
Volume240
Pages288-91
AuthorsSaudek V, Vincendon P, Do QT, Atkinson RA, Sklenar V, Pelton PD, Piriou F, Ganzhorn AJ
Title7Li nuclear-magnetic-resonance study of lithium binding to myo-inositolmonophosphatase.
[15]
PubMed ID9435892
JournalJ Med Chem
Year1997
Volume40
Pages4208-21
AuthorsPiettre SR, Andre C, Chanal MC, Ducep JB, Lesur B, Piriou F, Raboisson P, Rondeau JM, Schelcher C, Zimmermann P, Ganzhorn AJ
TitleMonoaryl- and bisaryldihydroxytropolones as potent inhibitors of inositol monophosphatase.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
JournalPRotein Eng
Year1997
Volume10
Pages61
AuthorsGanzhorn AJ, Rondeau JM
TitleStructure of an enzyme-substrate complex and the catalytic mechanism of human brain myo-inositol monophosphatase.
Related PDB1awb
Related Swiss-protP29218
[17]
PubMed ID9647837
JournalAppl Environ Microbiol
Year1998
Volume64
Pages2609-15
AuthorsChen L, Roberts MF
TitleCloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme.
[18]
PubMed ID9853417
JournalBiol Pharm Bull
Year1998
Volume21
Pages1218-21
AuthorsTsuda J, Kimura T, Tanino H, Shimohama S, Fujimoto S
TitleCharacterization of high- and low-molecular weight zinc-dependent acid phosphatases in bovine liver.
[19]
PubMed ID9988525
JournalJ Protein Chem
Year1998
Volume17
Pages789-97
AuthorsLau CK, Lo SC, Li W, Churchich DR, Kwok F, Churchich JE
TitlePartially folded conformations of inositol monophosphatase endowed with catalytic activity.
[20]
PubMed ID11828418
JournalChembiochem
Year2000
Volume1
Pages262-71
AuthorsMiller DJ, Beaton MW, Wilkie J, Gani D
TitleThe 6-OH group of D-inositol 1-phosphate serves as an H-bond donor in the catalytic hydrolysis of the phosphate ester by inositol monophosphatase.
[21]
PubMed ID10656801
JournalJ Mol Biol
Year2000
Volume295
Pages927-38
AuthorsAlbert A, Yenush L, Gil-Mascarell MR, Rodriguez PL, Patel S, Martinez-Ripoll M, Blundell TL, Serrano R
TitleX-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity.
[22]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL IONS.
PubMed ID11062561
JournalNat Struct Biol
Year2000
Volume7
Pages1046-50
AuthorsStec B, Yang H, Johnson KA, Chen L, Roberts MF
TitleMJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase.
Related PDB1dk4
Related Swiss-protQ57573
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed ID11170378
JournalBiochemistry
Year2001
Volume40
Pages618-30
AuthorsJohnson KA, Chen L, Yang H, Roberts MF, Stec B
TitleCrystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities.
Related PDB1g0h,1g0i
Related Swiss-protQ57573
[24]
PubMed ID11914086
JournalBiochemistry
Year2002
Volume41
Pages4392-8
AuthorsNigou J, Dover LG, Besra GS
TitlePurification and biochemical characterization of Mycobacterium tuberculosis SuhB, an inositol monophosphatase involved in inositol biosynthesis.
[25]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL IONS.
PubMed ID11940584
JournalJ Biol Chem
Year2002
Volume277
Pages22863-74
AuthorsStieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B
TitleCrystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop.
Related PDB1lbv,1lbw,1lbx,1lby,1lbz
Related Swiss-protO30298
[26]
PubMed ID11882005
JournalJ Med Chem
Year2002
Volume45
Pages1363-73
AuthorsFauroux CM, Lee M, Cullis PM, Douglas KT, Gore MG, Freeman S
TitleStereochemistry at phosphorus of the reaction catalyzed by myo-inositol monophosphatase.
[27]
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.
[28]
PubMed ID15858264
JournalActa Crystallogr D Biol Crystallogr
Year2005
Volume61
Pages545-55
AuthorsGill R, Mohammed F, Badyal R, Coates L, Erskine P, Thompson D, Cooper J, Gore M, Wood S
TitleHigh-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy.
Related PDB2bji
[29]
PubMed ID15715947
JournalJ Biochem Mol Biol
Year2005
Volume38
Pages58-64
AuthorsKim DW, Hong JW, Eum WS, Choi HS, Choi SH, Kim SY, Lee BR, An JJ, Lee SH, Lee SR, Kwon OS, Kwon HY, Cho SW, Lee KS, Park J, Choi SY
TitleInactivation of brain myo-inositol monophosphate phosphatase by pyridoxal-5'-phosphate.

comments
This enzyme belongs to the inositol monophosphatase family. Although this enzyme binds only two magnesium ions according to Swissprot data, it might binds a third ion. The catalytic mechanism of this enzyme seems to be similar to that of a homologous enzyme, 3'(2'),5'-bisphosphate nucleotidase (E.C. 3.1.3.7; D00148 in EzCatDB).
According to the literature [7], [8], [10], [20] & [28], the reaction proceeds by SN2-like mechanism as follows:
(1) Asp47 (of 1awb) acts as the general base to activate a water through Thr95 (probably acting as a proton shuttle). In addition, Magnesium-1, which binds the water and 1-phosphate of substrate, also activates the water probably by lowering its pKa. (If the third magnesium ion is available, it may assists the role of the magnesium-1).
(2) The activated water makes a nucleophilic attack on the phosphate group, leading to a trigonal bipyramidal transition state. This transition state is stabilized by Magnesium-1 and -2 ions. (Here, magnesium-2 stabilizes the negative charge developed on the leaving group.) Moreover, the mainchain amide groups of Gly94/Thr95 may stabilize the transition state (see [7]).
(3) The target bond, phosphoester bond, is broken.
(4) Another water, which is bound to 6-hydroxyl group of product, myo-inositol, seems to act as a acid to protonate the leaving 1-oxygen, through 6-hydroxyl group.

createdupdated
2005-08-052009-02-26


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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