Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of α- but not of β-, γ- and ζ-carbonic anhydrases

被引:46
作者
Innocenti, Alessio
Supuran, Claudiu T. [1 ]
机构
[1] Univ Florence, Lab Chim Bioinorgan, Rm 188,Via Lastruccia 3, I-50019 Florence, Italy
关键词
Carbonic anhydrase; Esterase; CO2; hydrase; Phosphatase; Paraoxon; Metalloenzyme; THALASSIOSIRA-WEISSFLOGII; THERAPEUTIC APPLICATIONS; HELICOBACTER-PYLORI; MARINE DIATOMS; CLASS ENZYME; ACTIVE-SITE; INHIBITORS; TARGET; IX; SULFONAMIDES;
D O I
10.1016/j.bmcl.2010.08.110
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to alpha-, beta-, gamma- and zeta-classes and from various organisms, ranging from the bacteria, archaea to eukarya domains, were investigated for their esterase/phosphatase activity with 4-nitrophenyl acetate, 4-nitrophenyl phosphate and paraoxon as substrates. Only alpha-CAs showed esterase/phosphatase activity, whereas enzymes belonging to the beta-, gamma- and zeta-classes were completely devoid of such activity. Paraoxon, the metabolite of the organophosphorus insecticide parathione, was a much better substrate for several human/murine alpha-CA isoforms (CA I, II and XIII), with k(cat)/K-M in the range of 2681.6-4474.9 M (1) s (1), compared to 4-nitrophenyl phosphate (k(cat)/K-M of 14.9-1374.4 M (1) s (1)). (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:6208 / 6212
页数:5
相关论文
共 61 条
[1]   Human monoclonal antibodies targeting carbonic anhydrase IX for the molecular imaging of hypoxic regions in solid tumours [J].
Ahlskog, J. K. J. ;
Schliemann, C. ;
Marlind, J. ;
Qureshi, U. ;
Ammar, A. ;
Pedley, R. B. ;
Neri, D. .
BRITISH JOURNAL OF CANCER, 2009, 101 (04) :645-657
[2]   In vivo targeting of tumor-associated carbonic anhydrases using acetazolamide derivatives [J].
Ahlskog, Julia K. J. ;
Dumelin, Christoph E. ;
Truessel, Sabrina ;
Marlind, Jessica ;
Neri, Dario .
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2009, 19 (16) :4851-4856
[3]  
Alterio V., 2009, DRUG DESIGN ZINC ENZ, P73
[4]   Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX [J].
Alterio, Vincenzo ;
Hilvo, Mika ;
Di Fiore, Anna ;
Supuran, Claudiu T. ;
Pan, Peiwen ;
Parkkila, Seppo ;
Scaloni, Andrea ;
Pastorek, Jaromir ;
Pastorekova, Silvia ;
Pedone, Carlo ;
Scozzafava, Andrea ;
Monti, Simona Maria ;
De Simone, Giuseppina .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (38) :16233-16238
[5]   Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF3- rather than by phosphoranes [J].
Baxter, Nicola J. ;
Bowler, Matthew W. ;
Alizadeh, Tooba ;
Cliff, Matthew J. ;
Hounslow, Andrea M. ;
Wu, Bin ;
Berkowitz, David B. ;
Williams, Nicholas H. ;
Blackburn, G. Michael ;
Waltho, Jonathan P. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (10) :4555-4560
[6]   Carbonic anhydrase inhibitors: Synthesis of water-soluble, topically effective intraocular pressure lowering aromatic/heterocyclic sulfonamides containing 8-quinoline-sulfonyl moieties: Is the tail more important than the ring? [J].
Borras, J ;
Scozzafava, A ;
Menabuoni, L ;
Mincione, F ;
Briganti, F ;
Mincione, G ;
Supuran, CT .
BIOORGANIC & MEDICINAL CHEMISTRY, 1999, 7 (11) :2397-2406
[7]   Why did Nature select phosphate for its dominant roles in biology? [J].
Bowler, Matthew W. ;
Cliff, Matthew J. ;
Waltho, Jonathan P. ;
Blackburn, G. Michael .
NEW JOURNAL OF CHEMISTRY, 2010, 34 (05) :784-794
[8]  
BROWN HV, 1950, ARCH INDHYG OCC MED, V1, P633
[9]   Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis [J].
Cliff, Matthew J. ;
Bowler, Matthew W. ;
Varga, Andrea ;
Marston, James P. ;
Szabo, Judit ;
Hounslow, Andrea M. ;
Baxter, Nicola J. ;
Blackburn, G. Michael ;
Vas, Maria ;
Waltho, Jonathan P. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2010, 132 (18) :6507-6516
[10]   The active site structure of Thalassiosira weissflogii carbonic anhydrase 1 [J].
Cox, EH ;
McLendon, GL ;
Morel, FMM ;
Lane, TW ;
Prince, RC ;
Pickering, IJ ;
George, GN .
BIOCHEMISTRY, 2000, 39 (40) :12128-12130