Tartrate-resistant acid phosphatase

ACP5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACP5, HPAP, SPENCDI, TRAP, TRACP5a, TRACP5b, TrATPase, acid phosphatase 5, tartrate resistant, TRAcP
External IDsOMIM: 171640; MGI: 87883; HomoloGene: 115578; GeneCards: ACP5; OMA:ACP5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

54

11433

Ensembl

ENSG00000102575

ENSMUSG00000001348

UniProt

P13686

Q05117

RefSeq (mRNA)

NM_001111034
NM_001111035
NM_001111036
NM_001611
NM_001322023

NM_001102404
NM_001102405
NM_007388

RefSeq (protein)

NP_001104504
NP_001104505
NP_001104506
NP_001308952
NP_001602

NP_001095874
NP_001095875
NP_031414

Location (UCSC)Chr 19: 11.57 – 11.58 MbChr 9: 22.04 – 22.05 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5) or TRAP5b, is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6–9.5), and optimal activity in acidic conditions. TRAP is synthesized as latent proenzyme and activated by proteolytic cleavage and reduction. It is differentiated from other mammalian acid phosphatases by its resistance to inhibition by tartrate and by its molecular weight.

The mechanism of phosphate ester hydrolysis by TRAP is through a nucleophilic attack mechanism, whereby, catalysis occurs with the binding of a phosphate-substrate to the Fe2+ in the active site of TRAP. This is then followed by a nucleophilic attack by a hydroxide ligand on the bound phosphorus atom, resulting in cleavage of the phosphate ester bond and production of an alcohol. The exact identity and mechanism of the hydroxide ligand is unclear, but it is thought to be either a hydroxide that bridges the metal ions within the active site or a terminal hydroxide bound to Fe3+, with conflicting reports for both mechanisms.