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Synonyms
acid phosphatase, tartrate-resistant acid phosphatase, prostatic acid phosphatase, tracp, acpase, uteroferrin, tracp 5b, phosphatidic acid phosphatase, tracp5b, pp2a phosphatase,
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acid monophosphatase
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acid nucleoside diphosphate phosphatase
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acid phosphatase PI
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isozyme
Acid phosphatase PII
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acid phosphatase PIIa
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isozyme, exhibits phytasic activity
acid phosphatase PIIb
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isozyme
acid phosphohydrolase
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acid phosphomoesterase
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acid phosphomonoester hydrolase
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acid phosphotyrosine phosphatase
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Adipocyte acid phosphatase, isozyme alpha
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Adipocyte acid phosphatase, isozyme beta
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APase isoform
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isoform 2
class-A bacterial non-specific acid phosphatases
colorless acid phosphatase
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erythrocyte-specific acid phosphatase
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ESAP, isozyme
glycerophosphatase
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high molecular weight acid phosphatase
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histidine acid phosphatase
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human prostatic acid phosphatase
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intracellular acid phosphatase
KhACP
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shows also chloroperoxidase activity
latex purple acid phosphatase
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lipoprotein e
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class C acid phosphatase
lipoprotein e acid phosphatase
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low acid phosphatase 3
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low molecular mass acid phosphatase
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low molecular weight acid phosphatase
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Low molecular weight phosphotyrosine protein phosphatase
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lysophosphatidic acid phosphatase
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membrane-bound acid phosphatase
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Minor phosphate-irrepressible acid phosphatase
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non-specific acid phosphatase
nucleotide pyrophosphatase/phosphodiesterase
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orthophosphoric monoester phosphohydrolase
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orthophosphoric monoester phosphohydrolase (acid optimum)
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orthophosphoric-monoester phosphohydrolase
pH 2.1 optimum acid phosphatase
pH 2.5 acid phosphatase
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pH 6-optimum acid phosphatase
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phosphate-repressible acid phosphatase
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phosphatidic acid phosphatase
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phosphohydrolase of orthophosphoric acid monoesters (acid optimum)
phosphomonoesterase
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phosphotyrosine phosphatase
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pi-starvation inducible purple acid phosphatase
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PP2A phosphatase
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i.e. isozyme 2
prostate acid phosphatase
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prostatic acid phosphatase
purple acid phosphatase 10
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purple acid phosphatase 12-1
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purple acid phosphatase 12-2
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purple acid phosphatase 12-3
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purple acid phosphatase 12-4
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purple acid phosphatase 12-5
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purple acid phosphatase 12-6
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purple acid phosphatase 12-7
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purple acid phosphatase PvPAP3
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respiratory burst-inhibiting acid phosphatase
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rnhC
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bifunctional enzyme with RNase H (N-terminus) and acid phosphatase (C-terminus) activities
secreted acid phosphatase
serum tartrate-resistant acid phosphatase
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Stationary-phase survival protein surE
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Tartrate-resistant acid ATPase
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tartrate-resistant acid phosphatase
thiamin-repressible acid phosphatase
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type-5 tartrate-resistant phosphatase
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vegetative storage protein alpha
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acid phosphatase
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acid phosphatase
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10 isoforms separated by isoelectric focusing (pI 4.7-7.9)
acid phosphatase A
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acid phosphatase I
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acid phosphatase II
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acid phosphatase II
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acid phosphatase III
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acid phosphatase III
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acid phosphatase MapA
autotransporter with acid phosphatase activity
acid phosphatase MapA
autotransporter with acid phosphatase activity
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acid phosphatase MapA
autotransporter with acid phosphatase activity
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acid phosphatase MapA
autotransporter with acid phosphatase activity
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acid phosphatase MapA
autotransporter with acid phosphatase activity
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acid phosphatase MapA
autotransporter with acid phosphatase activity
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ACP
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ACP1
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Acp5
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AcPase
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ACPase II
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AP
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APase
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APase
Musa cavendishii
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AphA
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Apho1p
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bNSAP
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class C acid phosphatase
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class C acid phosphatase
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class C acid phosphatase
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class-A bacterial non-specific acid phosphatases
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class-A bacterial non-specific acid phosphatases
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IAP
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intracellular acid phosphatase
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intracellular acid phosphatase
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major acid phosphatase
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MAP
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mAPA
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NapE
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non-specific acid phosphatase
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non-specific acid phosphatase
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non-specific acid phosphatase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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orthophosphoric-monoester phosphohydrolase
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PAP
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PAP1
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PAP10
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PAP26
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pH 2.1 optimum acid phosphatase
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pH 2.1 optimum acid phosphatase
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PhoN
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phosphohydrolase of orthophosphoric acid monoesters (acid optimum)
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phosphohydrolase of orthophosphoric acid monoesters (acid optimum)
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prostatic acid phosphatase
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prostatic acid phosphatase
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prostatic acid phosphatase
secretory isoform
purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
O24319
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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purple acid phosphatase
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rkbPAP
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rkbPAP
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red kidney bean PAP
SAP1
intracellular acid phosphatase
SAP2
extracellular acid phosphatase
secreted acid phosphatase
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secreted acid phosphatase
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tartrate-resistant acid phosphatase
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tartrate-resistant acid phosphatase
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tartrate-resistant acid phosphatase
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tartrate-resistant acid phosphatase
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TRAP, isozyme
tartrate-resistant acid phosphatase
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tartrate-resistant acid phosphatase
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tartrate-resistant acid phosphatase
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TRAP
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type 5 acid phosphatase
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type 5 acid phosphatase
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type 5 acid phosphatase
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uteroferrin
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additional information
the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases
additional information
the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases
additional information
the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases
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additional information
VSPalpha belongs to the haloacid dehalogenase superfamily
additional information
the enzyme belongs to the family of binuclear metalloenzymes
additional information
the colorless acid phosphatase is distinct from the purple acid phosphatase
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a phosphate monoester + H2O = an alcohol + phosphate
a phosphate monoester + H2O = an alcohol + phosphate
formation of a covalent phosphoryl-enzyme intermediate, kinetic pattern of a pseudo uni-bi hydrolytic two-step reaction mechanism
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a phosphate monoester + H2O = an alcohol + phosphate
active site structure analysis, substrate binding, H295 and E365 are involved in substrate orientation and stabilization of the transition state, oxygen binding and bridging at the metal ion center, overview, reaction mechanism
a phosphate monoester + H2O = an alcohol + phosphate
Asn91 and His92 are active site residues which interact with the loop residue Asp146, this interaction and substrate positioning by His92 is important for catalysis, Asn91 ia a ligand to the divalent metal of the mixed-valent di-iron center
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a phosphate monoester + H2O = an alcohol + phosphate
detailed structure-based catalytic mechanism
a phosphate monoester + H2O = an alcohol + phosphate
modelling of substrate binding in the active site
a phosphate monoester + H2O = an alcohol + phosphate
regioselective and stereospecific phosphorylation of diverse substrates by the acid phosphatase from Shigella flexneri and Salmonella enterica
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a phosphate monoester + H2O = an alcohol + phosphate
regioselective and stereospecific phosphorylation of diverse substrates by the acid phosphatase from Shigella flexneri and Salmonella enterica
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a phosphate monoester + H2O = an alcohol + phosphate
the enzyme is a Zn-metallophosphatase containing an essential zinc ion in the active site
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a phosphate monoester + H2O = an alcohol + phosphate
the dephosphorylation of phosphotyrosine by PAP is a two-step process: the first step involves the transfer of a phosphate group from the substrate to the histidine (His12). A number of quantum models are constructed containing various residues that are thought to play a role in the mechanism. In all these models, the transition state displays an associative character. The transition state is stabilized by three active site arginines (Arg11, Arg15, and Arg79), two of which belong to the conserved motif (RHGXRXP). His12 can act as a nucleophile. The enzyme is further characterized by a His257-Asp258 motif. Asp258 acts as a proton donor which becomes protonated when the substrate enters the binding pocket. The transfer of a proton from Asp258 to the leaving group is possibly mediated by a water molecule in the active site. The importance of His257 in lowering the energy barrier for the nucleophilic attack is shown
3.1.3.2 acid phosphatase
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