Literature DB >> 2394317

An enzyme with a double identity: purple acid phosphatase and tartrate-resistant acid phosphatase.

J B Vincent1, B A Averill.   

Abstract

The tartrate-resistant acid phosphatases or purple acid phosphatases constitute a class of related mammalian enzymes. Spectroscopic and magnetic studies have revealed that the purple phosphatases contain a novel dinuclear iron active site that is responsible for the purple color. More biologically and biomedically oriented research has shown that the tartrate-resistant acid phosphatases generally occur in osteoclasts and white blood cells, where they appear to be localized in lysosomes or similar organelles. Despite the different names given the enzymes by researchers in the two fields, recent sequence determinations and immunological studies indicate that the enzymes are identical. The status of research in both fields is reviewed in an attempt to present a unified picture of the structure, function, and mode of action of these unique metalloproteins.

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Year:  1990        PMID: 2394317     DOI: 10.1096/fasebj.4.12.2394317

Source DB:  PubMed          Journal:  FASEB J        ISSN: 0892-6638            Impact factor:   5.191


  10 in total

1.  Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases.

Authors:  J Ljusberg; B Ek-Rylander; G Andersson
Journal:  Biochem J       Date:  1999-10-01       Impact factor: 3.857

2.  Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower.

Authors:  Huifen Zhu; Weiqiang Qian; Xuzhong Lu; Dongping Li; Xin Liu; Kunfan Liu; Daowen Wang
Journal:  Plant Mol Biol       Date:  2005-11       Impact factor: 4.076

3.  Probing the toxic mechanism of bisphenol A with acid phosphatase at the molecular level.

Authors:  Mengchen Xu; Rui Zhang; Wei Song; Wansong Zong; Rutao Liu
Journal:  Environ Sci Pollut Res Int       Date:  2018-02-08       Impact factor: 4.223

4.  A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase.

Authors:  Marian Seto; Marc Whitlow; Margaret A McCarrick; Subha Srinivasan; Ying Zhu; Rene Pagila; Robert Mintzer; David Light; Anthony Johns; Janet A Meurer-Ogden
Journal:  Protein Sci       Date:  2004-12       Impact factor: 6.725

5.  Biochemical and molecular characterization of PvPAP3, a novel purple acid phosphatase isolated from common bean enhancing extracellular ATP utilization.

Authors:  Cuiyue Liang; Jiang Tian; Hon-Ming Lam; Boon Leong Lim; Xiaolong Yan; Hong Liao
Journal:  Plant Physiol       Date:  2009-12-02       Impact factor: 8.340

6.  Biochemical Characterization and Subcellular Localization of the Red Kidney Bean Purple Acid Phosphatase.

Authors:  A. G. Cashikar; R. Kumaresan; N. M. Rao
Journal:  Plant Physiol       Date:  1997-07       Impact factor: 8.340

7.  The glycosylphosphatidylinositol-anchored phosphatase from Spirodela oligorrhiza is a purple acid phosphatase.

Authors:  H Nakazato; T Okamoto; M Nishikoori; K Washio; N Morita; K Haraguchi; G A Thompson; H Okuyama
Journal:  Plant Physiol       Date:  1998-11       Impact factor: 8.340

Review 8.  A brief history of iron metabolism.

Authors:  J B Neilands
Journal:  Biol Met       Date:  1991

9.  An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro.

Authors:  Arnaud Hecker; Nicolas Leulliot; Danièle Gadelle; Marc Graille; Anthony Justome; Pierre Dorlet; Céline Brochier; Sophie Quevillon-Cheruel; Eric Le Cam; Herman van Tilbeurgh; Patrick Forterre
Journal:  Nucleic Acids Res       Date:  2007-08-30       Impact factor: 16.971

10.  How protein targeting to primary plastids via the endomembrane system could have evolved? A new hypothesis based on phylogenetic studies.

Authors:  Przemysław Gagat; Andrzej Bodył; Paweł Mackiewicz
Journal:  Biol Direct       Date:  2013-07-11       Impact factor: 4.540

  10 in total

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