EzCatDB: S00363

DB codeS00363
RLCP classification1.15.30200.84
CATH domainDomain 13.40.50.1240Catalytic domain
E.C.3.1.3.2
CSA1rpt

CATH domainRelated DB codes (homologues)
3.40.50.1240S00365,S00366,D00460,D00514

Enzyme Name
Swiss-protKEGG

P20646P15309
Protein nameProstatic acid phosphataseProstatic acid phosphataseacid phosphatase
acid phosphomonoesterase
phosphomonoesterase
glycerophosphatase
acid monophosphatase
acid phosphohydrolase
acid phosphomonoester hydrolase
uteroferrin
acid nucleoside diphosphate phosphatase
orthophosphoric-monoester phosphohydrolase (acid optimum)
SynonymsEC 3.1.3.2
EC 3.1.3.2

KEGG pathways
MAP codePathways
MAP00361gamma-Hexachlorocyclohexane degradation
MAP00740Riboflavin metabolism

Swiss-prot:Accession NumberP20646P15309
Entry namePPAP_RATPPAP_HUMAN
ActivityA phosphate monoester + H(2)O = an alcohol + phosphate.A phosphate monoester + H(2)O = an alcohol + phosphate.
SubunitHomodimer.Homodimer.
Subcellular location

Cofactor



SubstratesProducts
KEGG-idC01153C00001C00069C00009
CompoundOrthophosphoric monoesterH2OAlcoholOrthophosphate
Typecarbohydrate,phosphate group/phosphate ionH2Ocarbohydratephosphate group/phosphate ion
1rpaAUnbound
UnboundUnbound
1rptAUnbound
UnboundAnalogue:VO4
1nd5AAnalogue:2BF
UnboundUnbound
1nd5BAnalogue:2BF
UnboundUnbound
1nd5CAnalogue:2BF
UnboundUnbound
1nd5DAnalogue:2BF
UnboundUnbound
2hpaAUnbound
UnboundUnbound
2hpaBUnbound
UnboundUnbound
2hpaCUnbound
UnboundUnbound
2hpaDUnbound
UnboundUnbound

Active-site residues
resource
literature [2],[3]
pdbCatalytic residues
1rpaAARG   11;ARG   15;ARG   79;HIS  257(Stabilizers);HIS   12;ASP  258
1rptAARG   11;ARG   15;ARG   79;HIS  257(Stabilizers);HIS   12;ASP  258
1nd5AARG   11;ARG   15;ARG   79;HIS  257(Stabilizers);HIS   12;ASP  258
1nd5BARG 1010;ARG 1014;ARG 1078;HIS 1255(Stabilizers);HIS 1011;ASP 1256
1nd5CARG 2010;ARG 2014;ARG 2078;HIS 2256(Stabilizers);HIS 2011;ASP 2257
1nd5DARG 3010;ARG 3014;ARG 3078;HIS 3256(Stabilizers);HIS 3011;ASP 3257
2hpaAARG 1011;ARG 1015;ARG 1079;HIS 1257(Stabilizers);HIS 1012;ASP 1258
2hpaBARG 2011;ARG 2015;ARG 2079;HIS 2257(Stabilizers);HIS 2012;ASP 2258
2hpaCARG 3011;ARG 3015;ARG 3079;HIS 3257(Stabilizers);HIS 3012;ASP 3258
2hpaDARG 4011;ARG 4015;ARG 4079;HIS 4257(Stabilizers);HIS 4012;ASP 4258

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.2, Fig.3, p.141-1423
[3]Fig.42
[6]p.111

references
[1]
CommentsX-ray crystallography
PubMed ID8407898
JournalJ Biol Chem
Year1993
Volume268
Pages20744-6
AuthorsLindqvist Y, Schneider G, Vihko P
TitleThree-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
Related PDB1rpa
[2]
CommentsX-ray crystallography
PubMed ID8168503
JournalEur J Biochem
Year1994
Volume221
Pages139-142
AuthorsLindqvist Y, Schneider G, Vihko P
TitleCrystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
Related PDB1rpt
[3]
Commentsactive site mutation, catalysis
PubMed ID8132635
JournalJ Biol Chem
Year1994
Volume269
Pages8971-8
AuthorsOstanin K, Saeed A, Van Etten RL
TitleHeterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site.
[4]
CommentsX-ray crystallography (2.9 Angstroms)
PubMed ID9804805
JournalJ Biol Chem
Year1998
Volume273
Pages30406-9
AuthorsLaCount MW, Handy G, Lebioda L
TitleStructural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.
Related PDB2hpa
[5]
CommentsImprovement of catalytic efficiency by site-directed mutagenesis
PubMed ID11051103
JournalArch Biochem Biophys
Year2000
Volume382
Pages105-12
AuthorsRodriguez E, Wood ZA, Karplus PA, Lei XG
TitleSite-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
[6]
CommentsX-ray crystallography (2.05 Angstroms)
Medline ID20122624
PubMed ID10655611
JournalNat Struct Biol
Year2000
Volume7
Pages108-13
AuthorsLim D, Golovan S, Forsberg CW, Jia Z
TitleCrystal structures of Escherichia coli phytase and its complex with phytate.
Related PDB1dkl,1dkm,1dkn,1dko,1dkp,1dkq
[7]
CommentsX-ray crystallography (3.1 Angstroms)
PubMed ID10639192
JournalProstate
Year2000
Volume42
Pages211-8
AuthorsJakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L
TitleCrystal structure of human prostatic acid phosphatase .

comments
According to the literature [2] and [3], His12 (of 1rpa/1rpt) acts as nucleophile, which attacks the phosphorous atom of the phosphate ester, whilst Asp258 protonates the leaving group. At the next stage, the deprotonated Asp258 abstracts proton from the water, which hydrolyzes the phosphorylated imidazole ring of His12 [2].
Moreover, the three positively charged arginine residues (Arg11, Arg15, Arg79) near His12 play an important role in the catalysis, as follows [2];
(1) The positive charged groups lower the pKa of the nucelophilic histidine (His12), so that the acidic phosphatase can function below pH 7.
(2) These groups will orient the phosphate group in a proper position so that the nucleophilic attack at the phosphorous atom can take place while the phosphorous-oxygen bond is cleaved.

createdupdated
2002-08-012009-02-26


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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