PDBsum entry 2cba

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Lyase(oxo-acid) PDB id
Jmol PyMol
Protein chain
258 a.a. *
Waters ×220
* Residue conservation analysis
PDB id:
Name: Lyase(oxo-acid)
Title: Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
Structure: Carbonic anhydrase ii. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
1.54Å     R-factor:   0.151    
Authors: K.Hakansson,M.Carlsson,L.A.Svensson,A.Liljas
Key ref:
K.Håkansson et al. (1992). Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J Mol Biol, 227, 1192-1204. PubMed id: 1433293 DOI: 10.1016/0022-2836(92)90531-N
01-Jun-92     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00918  (CAH2_HUMAN) -  Carbonic anhydrase 2
260 a.a.
258 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Carbonic anhydrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
= CO(2)
+ H(2)O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   11 terms 
  Biological process     angiotensin-mediated signaling pathway   22 terms 
  Biochemical function     protein binding     6 terms  


    Added reference    
DOI no: 10.1016/0022-2836(92)90531-N J Mol Biol 227:1192-1204 (1992)
PubMed id: 1433293  
Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.
K.Håkansson, M.Carlsson, L.A.Svensson, A.Liljas.
In order to obtain a better structural framework for understanding the catalytic mechanism of carbonic anhydrase, a number of inhibitor complexes of the enzyme were investigated crystallographically. The three-dimensional structure of free human carbonic anhydrase II was refined at pH 7.8 (1.54 A resolution) and at pH 6.0 (1.67 A resolution). The structure around the zinc ion was identical at both pH values. The structure of the zinc-free enzyme was virtually identical with that of the native enzyme, apart from a water molecule that had moved 0.9 A to fill the space that would be occupied by the zinc ion. The complexes with the anionic inhibitors bisulfite and formate were also studied at neutral pH. Bisulfite binds with one of its oxygen atoms, presumably protonized, to the zinc ion and replaces the zinc water. Formate, lacking a hydroxyl group, is bound with its oxygen atoms not far away from the position of the non-protonized oxygen atoms of the bisulfite complex, i.e. at hydrogen bond distance from Thr199 N and at a position between the zinc ion and the hydrophobic part of the active site. The result of these and other studies have implications for our view of the catalytic function of the enzyme, since virtually all inhibitors share some features with substrate, product or expected transition states. A reaction scheme where electrophilic activation of carbon dioxide plays an important role in the hydration reaction is presented. In the reverse direction, the protonized oxygen of the bicarbonate is forced upon the zinc ion, thereby facilitating cleavage of the carbon-oxygen bond. This is achieved by the combined action of the anionic binding site, which binds carboxyl groups, the side-chain of threonine 199, which discriminates between hydrogen bond donors and acceptors, and hydrophobic interaction between substrate and the active site cavity. The required proton transfer between the zinc water and His64 can take place through water molecules 292 and 318.
  Selected figure(s)  
Figure 1.
Figure 1. The molecules involved in he hydrogen bond chain between His64 an the zinc water molecule in native carbnic anhydrase at pH 7%. Distances and angles are; 64Nd' -2920HH-3180HH: (322 A. 196.7''. 2.73 A) and 2920HH-3180HH-2630HH: (2.7 A, lOS.l'', 2.79 A).
Figure 3.
Figure 3. A larger view than in Fig. 2 of the active site. Note the ydrophobic nature of the right hand sde of the cleft ith valins 121, 143 and 207, leucines 141 and 198 and tryptophan 209.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1992, 227, 1192-1204) copyright 1992.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21298147 F.Pannetier, G.Ohanessian, and G.Frison (2011).
Comparison between α- and β-carbonic anhydrases: can Zn(His)3(H2O) and Zn(His)(Cys)2(H2O) sites lead to equivalent enzymes?
  Dalton Trans, 40, 2696-2698.  
21072437 H.Fliegl, O.Lehtonen, D.Sundholm, and V.R.Kaila (2011).
Hydrogen-bond strengths by magnetically induced currents.
  Phys Chem Chem Phys, 13, 434-437.  
21212893 O.Amata, T.Marino, N.Russo, and M.Toscano (2011).
Catalytic activity of a ζ-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms.
  Phys Chem Chem Phys, 13, 3468-3477.  
20445237 C.A.Behnke, I.Le Trong, J.W.Godden, E.A.Merritt, D.C.Teller, J.Bajorath, and R.E.Stenkamp (2010).
Atomic resolution studies of carbonic anhydrase II.
  Acta Crystallogr D Biol Crystallogr, 66, 616-627.
PDB codes: 1lug 3k34
19765680 C.M.Maupin, and G.A.Voth (2010).
Proton transport in carbonic anhydrase: Insights from molecular simulation.
  Biochim Biophys Acta, 1804, 332-341.  
20141756 M.Lignell, and H.C.Becker (2010).
Recognition and binding of a helix-loop-helix peptide to carbonic anhydrase occurs via partly folded intermediate structures.
  Biophys J, 98, 425-433.  
20025241 S.Z.Fisher, A.Y.Kovalevsky, J.F.Domsic, M.Mustyakimov, R.McKenna, D.N.Silverman, and P.A.Langan (2010).
Neutron structure of human carbonic anhydrase II: implications for proton transfer.
  Biochemistry, 49, 415-421.
PDB code: 3kkx
19818877 T.K.Hurst, D.Wang, R.B.Thompson, and C.A.Fierke (2010).
Carbonic anhydrase II-based metal ion sensing: Advances and new perspectives.
  Biochim Biophys Acta, 1804, 393-403.  
19583303 B.S.Avvaru, S.A.Busby, M.J.Chalmers, P.R.Griffin, B.Venkatakrishnan, M.Agbandje-McKenna, D.N.Silverman, and R.McKenna (2009).
Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network.
  Biochemistry, 48, 7365-7372.
PDB code: 3gz0
19520834 B.Sjöblom, M.Polentarutti, and K.Djinovic-Carugo (2009).
Structural study of X-ray induced activation of carbonic anhydrase.
  Proc Natl Acad Sci U S A, 106, 10609-10613.
PDB codes: 2vva 2vvb
19706507 C.L.Berthold, H.Wang, S.Nordlund, and M.Högbom (2009).
Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.
  Proc Natl Acad Sci U S A, 106, 14247-14252.
PDB codes: 2woc 2wod 2woe
19634894 C.M.Maupin, J.Zheng, C.Tu, R.McKenna, D.N.Silverman, and G.A.Voth (2009).
Effect of active-site mutation at Asn67 on the proton transfer mechanism of human carbonic anhydrase II.
  Biochemistry, 48, 7996-8005.  
19438233 C.M.Maupin, R.McKenna, D.N.Silverman, and G.A.Voth (2009).
Elucidation of the proton transport mechanism in human carbonic anhydrase II.
  J Am Chem Soc, 131, 7598-7608.  
19588465 D.Aili, R.Selegård, L.Baltzer, K.Enander, and B.Liedberg (2009).
Colorimetric protein sensing by controlled assembly of gold nanoparticles functionalized with synthetic receptors.
  Small, 5, 2445-2452.  
19503918 D.Coquière, S.Le Gac, U.Darbost, O.Sénèque, I.Jabin, and O.Reinaud (2009).
Biomimetic and self-assembled calix[6]arene-based receptors for neutral molecules.
  Org Biomol Chem, 7, 2485-2500.  
19088994 G.Frison, and G.Ohanessian (2009).
Metal-histidine-glutamate as a regulator of enzymatic cycles: a case study of carbonic anhydrase.
  Phys Chem Chem Phys, 11, 374-383.  
19140795 J.M.Chambers, P.A.Hill, J.A.Aaron, Z.Han, D.W.Christianson, N.N.Kuzma, and I.J.Dmochowski (2009).
Cryptophane xenon-129 nuclear magnetic resonance biosensors targeting human carbonic anhydrase.
  J Am Chem Soc, 131, 563-569.  
19217874 R.Chiuri, G.Maiorano, A.Rizzello, L.L.del Mercato, R.Cingolani, R.Rinaldi, M.Maffia, and P.P.Pompa (2009).
Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.
  Biophys J, 96, 1586-1596.  
19185003 S.B.Moparthi, P.Hammarström, and U.Carlsson (2009).
A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding.
  Protein Sci, 18, 475-479.  
18671353 C.M.Maupin, M.G.Saunders, I.F.Thorpe, R.McKenna, D.N.Silverman, and G.A.Voth (2008).
Origins of enhanced proton transport in the Y7F mutant of human carbonic anhydrase II.
  J Am Chem Soc, 130, 11399-11408.  
19036170 F.Bootorabi, J.Jänis, J.Valjakka, S.Isoniemi, P.Vainiotalo, D.Vullo, C.T.Supuran, A.Waheed, W.S.Sly, O.Niemelä, and S.Parkkila (2008).
Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity.
  BMC Biochem, 9, 32.  
17631650 G.Frison, and G.Ohanessian (2008).
A comparative study of semiempirical, ab initio, and DFT methods in evaluating metal-ligand bond strength, proton affinity, and interactions between first and second shell ligands in Zn-biomimetic complexes.
  J Comput Chem, 29, 416-433.  
18461940 J.A.Aaron, J.M.Chambers, K.M.Jude, L.Di Costanzo, I.J.Dmochowski, and D.W.Christianson (2008).
Structure of a 129Xe-cryptophane biosensor complexed with human carbonic anhydrase II.
  J Am Chem Soc, 130, 6942-6943.
PDB code: 3cyu
18768466 J.F.Domsic, B.S.Avvaru, C.U.Kim, S.M.Gruner, M.Agbandje-McKenna, D.N.Silverman, and R.McKenna (2008).
Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II.
  J Biol Chem, 283, 30766-30771.
PDB codes: 3d92 3d93
18931408 J.Jeyakanthan, S.Rangarajan, P.Mridula, S.P.Kanaujia, Y.Shiro, S.Kuramitsu, S.Yokoyama, and K.Sekar (2008).
Observation of a calcium-binding site in the gamma-class carbonic anhydrase from Pyrococcus horikoshii.
  Acta Crystallogr D Biol Crystallogr, 64, 1012-1019.
PDB codes: 1v3w 1v67 2fko
18942852 J.Zheng, B.S.Avvaru, C.Tu, R.McKenna, and D.N.Silverman (2008).
Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.
  Biochemistry, 47, 12028-12036.
PDB codes: 3dv7 3dvb 3dvc 3dvd
  18323598 P.A.Mazumdar, D.Kumaran, S.Swaminathan, and A.K.Das (2008).
A novel acetate-bound complex of human carbonic anhydrase II.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 163-166.
PDB code: 1xeg
18335973 V.M.Krishnamurthy, G.K.Kaufman, A.R.Urbach, I.Gitlin, K.L.Gudiksen, D.B.Weibel, and G.M.Whitesides (2008).
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
  Chem Rev, 108, 946.  
18060825 Y.Jiang, J.T.Su, J.Zhang, X.Wei, Y.B.Yan, and H.M.Zhou (2008).
Reshaping the folding energy landscape of human carbonic anhydrase II by a single point genetic mutation Pro237His.
  Int J Biochem Cell Biol, 40, 776-788.  
18322527 Y.Xu, L.Feng, P.D.Jeffrey, Y.Shi, and F.M.Morel (2008).
Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms.
  Nature, 452, 56-61.
PDB codes: 3bob 3boc 3boe 3boh 3boj
17319695 C.M.Maupin, and G.A.Voth (2007).
Preferred orientations of His64 in human carbonic anhydrase II.
  Biochemistry, 46, 2938-2947.  
17071654 D.Bhatt, S.Z.Fisher, C.Tu, R.McKenna, and D.N.Silverman (2007).
Location of binding sites in small molecule rescue of human carbonic anhydrase II.
  Biophys J, 92, 562-570.
PDB codes: 2fnk 2fnm 2fnn
17665409 G.E.Höst, J.Razkin, L.Baltzer, and B.H.Jonsson (2007).
Combined enzyme and substrate design: grafting of a cooperative two-histidine catalytic motif into a protein targeted at the scissile bond in a designed ester substrate.
  Chembiochem, 8, 1570-1576.  
17202139 H.Shimahara, T.Yoshida, Y.Shibata, M.Shimizu, Y.Kyogoku, F.Sakiyama, T.Nakazawa, S.Tate, S.Y.Ohki, T.Kato, H.Moriyama, K.Kishida, Y.Tano, T.Ohkubo, and Y.Kobayashi (2007).
Tautomerism of histidine 64 associated with proton transfer in catalysis of carbonic anhydrase.
  J Biol Chem, 282, 9646-9656.  
17429993 J.M.Swanson, C.M.Maupin, H.Chen, M.K.Petersen, J.Xu, Y.Wu, and G.A.Voth (2007).
Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations.
  J Phys Chem B, 111, 4300-4314.  
17407539 N.Fabre, I.M.Reiter, N.Becuwe-Linka, B.Genty, and D.Rumeau (2007).
Characterization and expression analysis of genes encoding alpha and beta carbonic anhydrases in Arabidopsis.
  Plant Cell Environ, 30, 617-629.  
17545162 O.Azim-Zadeh, A.Hillebrecht, U.Linne, M.A.Marahiel, G.Klebe, K.Lingelbach, and J.Nyalwidhe (2007).
Use of biotin derivatives to probe conformational changes in proteins.
  J Biol Chem, 282, 21609-21617.  
17573429 S.Marino, K.Hayakawa, K.Hatada, M.Benfatto, A.Rizzello, M.Maffia, and L.Bubacco (2007).
Structural features that govern enzymatic activity in carbonic anhydrase from a low-temperature adapted fish, Chionodraco hamatus.
  Biophys J, 93, 2781-2790.  
17587158 S.Safarian, F.Bagheri, A.A.Moosavi-Movahedi, M.Amanlou, and N.Sheibani (2007).
Competitive inhibitory effects of acetazolamide upon interactions with bovine carbonic anhydrase II.
  Protein J, 26, 371-385.  
17441142 V.M.Krishnamurthy, B.R.Bohall, C.Y.Kim, D.T.Moustakas, D.W.Christianson, and G.M.Whitesides (2007).
Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II.
  Chem Asian J, 2, 94.  
16557501 A.Roy, and S.Taraphder (2006).
Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II.
  Biopolymers, 82, 623-630.  
17165785 D.Riccardi, P.König, X.Prat-Resina, H.Yu, M.Elstner, T.Frauenheim, and Q.Cui (2006).
"Proton holes" in long-range proton transfer reactions in solution and enzymes: A theoretical analysis.
  J Am Chem Soc, 128, 16302-16311.  
16617087 K.L.Gudiksen, I.Gitlin, D.T.Moustakas, and G.M.Whitesides (2006).
Increasing the net charge and decreasing the hydrophobicity of bovine carbonic anhydrase decreases the rate of denaturation with sodium dodecyl sulfate.
  Biophys J, 91, 298-310.  
16506782 K.M.Jude, A.L.Banerjee, M.K.Haldar, S.Manokaran, B.Roy, S.Mallik, D.K.Srivastava, and D.W.Christianson (2006).
Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity.
  J Am Chem Soc, 128, 3011-3018.
PDB codes: 2foq 2fos 2fou 2fov 2foy
16708362 N.Hirano, T.Sawasaki, Y.Tozawa, Y.Endo, and K.Takai (2006).
Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system.
  Proteins, 64, 343-354.  
16932811 S.Schenk, J.Notni, U.Köhn, K.Wermann, and E.Anders (2006).
Carbon dioxide and related heterocumulenes at zinc and lithium cations: bioinspired reactions and principles.
  Dalton Trans, (), 4191-4206.  
16006526 J.W.Schymkowitz, F.Rousseau, I.C.Martins, J.Ferkinghoff-Borg, F.Stricher, and L.Serrano (2005).
Prediction of water and metal binding sites and their affinities by using the Fold-X force field.
  Proc Natl Acad Sci U S A, 102, 10147-10152.  
15726624 M.Babor, H.M.Greenblatt, M.Edelman, and V.Sobolev (2005).
Flexibility of metal binding sites in proteins on a database scale.
  Proteins, 59, 221-230.  
15731384 M.Karlsson, and U.Carlsson (2005).
Protein adsorption orientation in the light of fluorescent probes: mapping of the interaction between site-directly labeled human carbonic anhydrase II and silica nanoparticles.
  Biophys J, 88, 3536-3544.  
16035867 P.Schaefer, D.Riccardi, and Q.Cui (2005).
Reliable treatment of electrostatics in combined QM/MM simulation of macromolecules.
  J Chem Phys, 123, 014905.  
15929995 R.Afrin, M.T.Alam, and A.Ikai (2005).
Pretransition and progressive softening of bovine carbonic anhydrase II as probed by single molecule atomic force microscopy.
  Protein Sci, 14, 1447-1457.  
14660577 D.A.Whittington, J.H.Grubb, A.Waheed, G.N.Shah, W.S.Sly, and D.W.Christianson (2004).
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.
  J Biol Chem, 279, 7223-7228.
PDB codes: 1rj5 1rj6
15342572 H.Richard, and J.W.Foster (2004).
Escherichia coli glutamate- and arginine-dependent acid resistance systems increase internal pH and reverse transmembrane potential.
  J Bacteriol, 186, 6032-6041.  
15340162 K.Sale, J.L.Faulon, G.A.Gray, J.S.Schoeniger, and M.M.Young (2004).
Optimal bundling of transmembrane helices using sparse distance constraints.
  Protein Sci, 13, 2613-2627.  
15377514 S.Ohta, M.T.Alam, H.Arakawa, and A.Ikai (2004).
Origin of mechanical strength of bovine carbonic anhydrase studied by molecular dynamics simulation.
  Biophys J, 87, 4007-4020.  
12632471 M.Elstner, Q.Cui, P.Munih, E.Kaxiras, T.Frauenheim, and M.Karplus (2003).
Modeling zinc in biomolecules with the self consistent charge-density functional tight binding (SCC-DFTB) method: applications to structural and energetic analysis.
  J Comput Chem, 24, 565-581.  
11976500 D.M.Duda, C.Yoshioka, L.Govindasamy, H.An, C.Tu, D.N.Silverman, and R.McKenna (2002).
Crystallization and preliminary X-ray analysis of human carbonic anhydrase III.
  Acta Crystallogr D Biol Crystallogr, 58, 849-852.  
12022873 S.B.Tikunova, J.A.Rall, and J.P.Davis (2002).
Effect of hydrophobic residue substitutions with glutamine on Ca(2+) binding and exchange with the N-domain of troponin C.
  Biochemistry, 41, 6697-6705.  
12056894 S.Huang, B.Sjöblom, A.E.Sauer-Eriksson, and B.H.Jonsson (2002).
Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant.
  Biochemistry, 41, 7628-7635.
PDB codes: 1lg5 1lg6 1lgd
11493685 D.A.Whittington, A.Waheed, B.Ulmasov, G.N.Shah, J.H.Grubb, W.S.Sly, and D.W.Christianson (2001).
Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells.
  Proc Natl Acad Sci U S A, 98, 9545-9550.
PDB codes: 1jcz 1jd0
11327835 D.Duda, C.Tu, M.Qian, P.Laipis, M.Agbandje-McKenna, D.N.Silverman, and R.McKenna (2001).
Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II.
  Biochemistry, 40, 1741-1748.
PDB codes: 1g0e 1g0f
11371461 M.Persson, J.R.Harbridge, P.Hammarström, R.Mitri, L.G.Mårtensson, U.Carlsson, G.R.Eaton, and S.S.Eaton (2001).
Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II.
  Biophys J, 80, 2886-2897.  
11371460 P.Hammarström, R.Owenius, L.G.Mårtensson, U.Carlsson, and M.Lindgren (2001).
High-resolution probing of local conformational changes in proteins by the use of multiple labeling: unfolding and self-assembly of human carbonic anhydrase II monitored by spin, fluorescent, and chemical reactivity probes.
  Biophys J, 80, 2867-2885.  
10998050 B.Elleby, B.Sjöblom, C.Tu, D.N.Silverman, and S.Lindskog (2000).
Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein.
  Eur J Biochem, 267, 5908-5915.  
11018657 G.G.Montich (2000).
Partly folded states of bovine carbonic anhydrase interact with zwitterionic and anionic lipid membranes.
  Biochim Biophys Acta, 1468, 115-126.  
11063570 J.W.Vince, U.Carlsson, and R.A.Reithmeier (2000).
Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II.
  Biochemistry, 39, 13344-13349.  
10978542 K.S.Smith, and J.G.Ferry (2000).
Prokaryotic carbonic anhydrases.
  FEMS Microbiol Rev, 24, 335-366.  
11123909 L.Norregaard, I.Visiers, C.J.Loland, J.Ballesteros, H.Weinstein, and U.Gether (2000).
Structural probing of a microdomain in the dopamine transporter by engineering of artificial Zn2+ binding sites.
  Biochemistry, 39, 15836-15846.  
10747009 M.S.Kimber, and E.F.Pai (2000).
The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases.
  EMBO J, 19, 1407-1418.
PDB code: 1ekj
  10794421 R.E.Burton, J.A.Hunt, C.A.Fierke, and T.G.Oas (2000).
Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.
  Protein Sci, 9, 776-785.  
10681531 S.Mitsuhashi, T.Mizushima, E.Yamashita, M.Yamamoto, T.Kumasaka, H.Moriyama, T.Ueki, S.Miyachi, and T.Tsukihara (2000).
X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration.
  J Biol Chem, 275, 5521-5526.
PDB code: 1ddz
10812023 S.Scheiner (2000).
Calculation of isotope effects from first principles.
  Biochim Biophys Acta, 1458, 28-42.  
10336637 B.Elleby, B.Sjöblom, and S.Lindskog (1999).
Changing the efficiency and specificity of the esterase activity of human carbonic anhydrase II by site-specific mutagenesis.
  Eur J Biochem, 262, 516-521.  
10872443 D.W.Christianson, and J.D.Cox (1999).
Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes.
  Annu Rev Biochem, 68, 33-57.  
10413479 J.A.Hunt, M.Ahmed, and C.A.Fierke (1999).
Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic core residues.
  Biochemistry, 38, 9054-9062.  
10354450 J.Gao, Q.Wu, J.Carbeck, Q.P.Lei, R.D.Smith, and G.M.Whitesides (1999).
Probing the energetics of dissociation of carbonic anhydrase-ligand complexes in the gas phase.
  Biophys J, 76, 3253-3260.  
  10515911 K.S.Smith, and J.G.Ferry (1999).
A plant-type (beta-class) carbonic anhydrase in the thermophilic methanoarchaeon Methanobacterium thermoautotrophicum.
  J Bacteriol, 181, 6247-6253.  
10551854 P.Hammarström, M.Persson, P.O.Freskgârd, L.G.Mârtensson, D.Andersson, B.H.Jonsson, and U.Carlsson (1999).
Structural mapping of an aggregation nucleation site in a molten globule intermediate.
  J Biol Chem, 274, 32897-32903.  
10413512 S.T.Liu, G.Howlett, and C.J.Barrow (1999).
Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease.
  Biochemistry, 38, 9373-9378.  
9635771 C.Tu, M.Qian, J.N.Earnhardt, P.J.Laipis, and D.N.Silverman (1998).
Properties of intramolecular proton transfer in carbonic anhydrase III.
  Biophys J, 74, 3182-3189.  
9667939 J.E.Coleman (1998).
Zinc enzymes.
  Curr Opin Chem Biol, 2, 222-234.  
  9865942 P.A.Boriack-Sjodin, S.Zeitlin, H.H.Chen, L.Crenshaw, S.Gross, A.Dantanarayana, P.Delgado, J.A.May, T.Dean, and D.W.Christianson (1998).
Structural analysis of inhibitor binding to human carbonic anhydrase II.
  Protein Sci, 7, 2483-2489.
PDB codes: 1bn1 1bn3 1bn4 1bnm 1bnn 1bnq 1bnt 1bnu 1bnv 1bnw
  9541386 T.Stams, Y.Chen, P.A.Boriack-Sjodin, J.D.Hurt, J.Liao, J.A.May, T.Dean, P.Laipis, D.N.Silverman, and D.W.Christianson (1998).
Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination.
  Protein Sci, 7, 556-563.
PDB codes: 1a42 2znc 3znc
9109672 D.Andersson, P.O.Freskgård, B.H.Jonsson, and U.Carlsson (1997).
Formation of local native-like tertiary structures in the slow refolding reaction of human carbonic anhydrase II as monitored by circular dichroism on tryptophan mutants.
  Biochemistry, 36, 4623-4630.  
9265618 F.Briganti, S.Mangani, P.Orioli, A.Scozzafava, G.Vernaglione, and C.T.Supuran (1997).
Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine.
  Biochemistry, 36, 10384-10392.
PDB code: 1avn
9252341 J.A.Hunt, and C.A.Fierke (1997).
Selection of carbonic anhydrase variants displayed on phage. Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics.
  J Biol Chem, 272, 20364-20372.  
9136875 P.Jonasson, G.Aronsson, U.Carlsson, and B.H.Jonsson (1997).
Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II.
  Biochemistry, 36, 5142-5148.  
  9371472 S.A.Braus-Stromeyer, G.Schnappauf, G.H.Braus, A.S.Gössner, and H.L.Drake (1997).
Carbonic anhydrase in Acetobacterium woodii and other acetogenic bacteria.
  J Bacteriol, 179, 7197-7200.  
9336012 S.Lindskog (1997).
Structure and mechanism of carbonic anhydrase.
  Pharmacol Ther, 74, 1.  
9054574 T.T.Baird, A.Waheed, T.Okuyama, W.S.Sly, and C.A.Fierke (1997).
Catalysis and inhibition of human carbonic anhydrase IV.
  Biochemistry, 36, 2669-2678.  
  8655508 B.E.Alber, and J.G.Ferry (1996).
Characterization of heterologously produced carbonic anhydrase from Methanosarcina thermophila.
  J Bacteriol, 178, 3270-3274.  
8639494 C.C.Huang,, C.A.Lesburg, L.L.Kiefer, C.A.Fierke, and D.W.Christianson (1996).
Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II.
  Biochemistry, 35, 3439-3446.
PDB codes: 1zsa 1zsb 1zsc
  8665839 C.Kisker, H.Schindelin, B.E.Alber, J.G.Ferry, and D.C.Rees (1996).
A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila.
  EMBO J, 15, 2323-2330.
PDB code: 1thj
8973657 H.Li, P.J.Sadler, and H.Sun (1996).
Rationalization of the strength of metal binding to human serum transferrin.
  Eur J Biochem, 242, 387-393.  
8987973 J.E.Jackman, K.M.Merz, and C.A.Fierke (1996).
Disruption of the active site solvent network in carbonic anhydrase II decreases the efficiency of proton transfer.
  Biochemistry, 35, 16421-16428.  
  8976556 K.Borén, P.O.Freskgård, and U.Carlsson (1996).
A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: impact on calculation of secondary structure content.
  Protein Sci, 5, 2479-2484.  
8987974 L.R.Scolnick, and D.W.Christianson (1996).
X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.
  Biochemistry, 35, 16429-16434.
PDB codes: 1uga 1ugb 1ugc 1ugd 1uge 1ugf 1ugg
8634241 L.S.Brinen, W.S.Willett, C.S.Craik, and R.J.Fletterick (1996).
X-ray structures of a designed binding site in trypsin show metal-dependent geometry.
  Biochemistry, 35, 5999-6009.
PDB codes: 1slu 1slv 1slw 1slx
8942978 T.Stams, S.K.Nair, T.Okuyama, A.Waheed, W.S.Sly, and D.W.Christianson (1996).
Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution.
  Proc Natl Acad Sci U S A, 93, 13589-13594.
PDB code: 1znc
7758465 C.Engstrand, B.H.Jonsson, and S.Lindskog (1995).
Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I.
  Eur J Biochem, 229, 696-702.  
7761440 J.A.Ippolito, T.T.Baird, S.A.McGee, D.W.Christianson, and C.A.Fierke (1995).
Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity.
  Proc Natl Acad Sci U S A, 92, 5017-5021.
PDB codes: 1ccs 1cct 1ccu
7479916 P.A.Boriack-Sjodin, R.W.Heck, P.J.Laipis, D.N.Silverman, and D.W.Christianson (1995).
Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design.
  Proc Natl Acad Sci U S A, 92, 10949-10953.
PDB codes: 1dmx 1dmy
8536678 R.J.Williams (1995).
Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins.
  Eur J Biochem, 234, 363-381.  
8528764 U.Carlsson, and B.H.Jonsson (1995).
Folding of beta-sheet proteins.
  Curr Opin Struct Biol, 5, 482-487.  
8306976 A.Liljas, K.Håkansson, B.H.Jonsson, and Y.Xue (1994).
Inhibition and catalysis of carbonic anhydrase. Recent crystallographic analyses.
  Eur J Biochem, 219, 1.  
7925414 I.M.Johansson, and C.Forsman (1994).
Solvent hydrogen isotope effects and anion inhibition of CO2 hydration catalysed by carbonic anhydrase from Pisum sativum.
  Eur J Biochem, 224, 901-907.  
8269932 I.M.Johansson, and C.Forsman (1993).
Kinetic studies of pea carbonic anhydrase.
  Eur J Biochem, 218, 439-446.  
8477723 S.K.Nair, and D.W.Christianson (1993).
Crystallographic studies of azide binding to human carbonic anhydrase II.
  Eur J Biochem, 213, 507-515.  
7901850 Y.Xue, A.Liljas, B.H.Jonsson, and S.Lindskog (1993).
Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II.
  Proteins, 17, 93.
PDB codes: 1cai 1caj 1cak 1cal 1cam
8436138 Z.Liang, Y.Xue, G.Behravan, B.H.Jonsson, and S.Lindskog (1993).
Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II.
  Eur J Biochem, 211, 821-827.  
1336460 S.Mangani, and K.Håkansson (1992).
Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions.
  Eur J Biochem, 210, 867-871.
PDB codes: 1can 1cao
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