Carbonic anhydrase 2

[1]. Anna Di Fiore, et al. Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties. Bioorg Med Chem Lett. 2007 Mar 15;17(6):1726-31. [Content Brief]

[2]. Gul N Shah, et al. Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation. Hum Mutat. 2004 Sep;24(3):272. [Content Brief]

[3]. Claudia Temperini, et al. Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct of N-hydroxysulfamide with isozyme II explains why this new zinc binding function is effective in the design of potent inhibitors. Bioorg Med Chem Lett. 2007 May 15;17(10):2795-801. [Content Brief]

[4]. Deepa Bhatt, et al. Proton transfer in a Thr200His mutant of human carbonic anhydrase II. Proteins. 2005 Nov 1;61(2):239-45. [Content Brief]

[5]. Bernardo V Alvarez, et al. Metabolon disruption: a mechanism that regulates bicarbonate transport. EMBO J. 2005 Jul 20;24(14):2499-511. [Content Brief]

[6]. J A Ippolito, et al. Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II. Biochemistry. 1993 Sep 28;32(38):9901-5. [Content Brief]

[7]. J F Krebs, et al. Conformational mobility of His-64 in the Thr-200----Ser mutant of human carbonic anhydrase II. Biochemistry. 1991 Sep 24;30(38):9153-60. [Content Brief]

[8]. Chingkuang Tu, et al. Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase. J Biol Chem. 2002 Oct 11;277(41):38870-6. [Content Brief]

[9]. Y Xue, et al. Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-. Proteins. 1993 Jan;15(1):80-7. [Content Brief]

[10]. Y Xue, et al. Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II. Proteins. 1993 Sep;17(1):93-106. [Content Brief]

[11]. J A Ippolito, et al. Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity. Proc Natl Acad Sci U S A. 1995 May 23;92(11):5017-21. [Content Brief]

[12]. Jiayin Zheng, et al. Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II. Biochemistry. 2008 Nov 18;47(46):12028-36. [Content Brief]

[13]. F Briganti, et al. Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?. J Biol Inorg Chem. 1999 Oct;4(5):528-36. [Content Brief]

[14]. Chu-Young Kim, et al. Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV. J Med Chem. 2002 Feb 14;45(4):888-93. [Content Brief]

[15]. J F Krebs, et al. Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II. J Biol Chem. 1993 Dec 25;268(36):27458-66. [Content Brief]

[16]. D Duda, et al. Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II. Biochemistry. 2001 Feb 13;40(6):1741-8. [Content Brief]

[17]. A Guerri, et al. Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction. Biochemistry. 2000 Oct 10;39(40):12391-7. [Content Brief]

[18]. S K Nair, et al. Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II. Biochemistry. 1993 May 4;32(17):4506-14. [Content Brief]

[19]. N B Tweedy, et al. Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant. Biochemistry. 1993 Oct 19;32(41):10944-9. [Content Brief]

[20]. Matthew D Lloyd, et al. First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors. Biochemistry. 2005 May 10;44(18):6858-66. [Content Brief]

[21]. S K Nair, et al. Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121. J Biol Chem. 1991 Sep 15;266(26):17320-5. [Content Brief]

[22]. Matthew D Lloyd, et al. Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent. Biochem J. 2005 Feb 1;385(Pt 3):715-20. [Content Brief]

[23]. Zoë Fisher, et al. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry. 2005 Feb 1;44(4):1097-105. [Content Brief]

[24]. F Briganti, et al. Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. Biochemistry. 1997 Aug 26;36(34):10384-92. [Content Brief]

[25]. Shenghua Huang, et al. Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant. Biochemistry. 2002 Jun 18;41(24):7628-35. [Content Brief]

[26]. S Mangani, et al. Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions. Eur J Biochem. 1992 Dec 15;210(3):867-71. [Content Brief]

[27]. C C Huang, et al. Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II. Biochemistry. 1996 Mar 19;35(11):3439-46. [Content Brief]

[28]. C A Lesburg, et al. Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity. Biochemistry. 1997 Dec 16;36(50):15780-91. [Content Brief]

[29]. Claudia Temperini, et al. Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators. Bioorg Med Chem Lett. 2005 Dec 1;15(23):5136-41. [Content Brief]

[30]. S Zoë Fisher, et al. Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II. Biochemistry. 2007 Mar 27;46(12):3803-13. [Content Brief]