Details for: CA2

Gene ID: 760

Symbol: CA2

Ensembl ID: ENSG00000104267

Description: carbonic anhydrase 2

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: 4.4
    Marker Score: 28050
  • Cell Name: enterocyte of colon (CL1000347)
    Fold Change: 3.85
    Marker Score: 5936.5
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 3.74
    Marker Score: 9433
  • Cell Name: colon epithelial cell (CL0011108)
    Fold Change: 3.37
    Marker Score: 10587
  • Cell Name: mucous neck cell (CL0000651)
    Fold Change: 2.95
    Marker Score: 6701
  • Cell Name: serous secreting cell (CL0000313)
    Fold Change: 2.95
    Marker Score: 1177
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 2.85
    Marker Score: 3025
  • Cell Name: kidney collecting duct intercalated cell (CL1001432)
    Fold Change: 2.83
    Marker Score: 4687
  • Cell Name: Mueller cell (CL0000636)
    Fold Change: 2.63
    Marker Score: 3649
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 2.55
    Marker Score: 3606
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: 2.5
    Marker Score: 5994
  • Cell Name: renal intercalated cell (CL0005010)
    Fold Change: 2.16
    Marker Score: 1153
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 1.95
    Marker Score: 6938.5
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 1.79
    Marker Score: 4071
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 1.78
    Marker Score: 2834
  • Cell Name: pneumocyte (CL0000322)
    Fold Change: 1.77
    Marker Score: 2837
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 1.76
    Marker Score: 1758
  • Cell Name: osteoclast (CL0000092)
    Fold Change: 1.74
    Marker Score: 868
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 1.71
    Marker Score: 1781
  • Cell Name: type II pneumocyte (CL0002063)
    Fold Change: 1.71
    Marker Score: 11176.5
  • Cell Name: tracheobronchial serous cell (CL0019001)
    Fold Change: 1.71
    Marker Score: 624.5
  • Cell Name: peptic cell (CL0000155)
    Fold Change: 1.67
    Marker Score: 698
  • Cell Name: proerythroblast (CL0000547)
    Fold Change: 1.65
    Marker Score: 1119
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 1.64
    Marker Score: 4402.5
  • Cell Name: NKp44-negative group 3 innate lymphoid cell, human (CL0001080)
    Fold Change: 1.6
    Marker Score: 352
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 1.48
    Marker Score: 6150
  • Cell Name: mural cell (CL0008034)
    Fold Change: 1.47
    Marker Score: 168330
  • Cell Name: enterocyte (CL0000584)
    Fold Change: 1.45
    Marker Score: 6963
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 1.43
    Marker Score: 834
  • Cell Name: primitive red blood cell (CL0002355)
    Fold Change: 1.4
    Marker Score: 1052.5
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 1.39
    Marker Score: 345
  • Cell Name: mammary gland epithelial cell (CL0002327)
    Fold Change: 1.34
    Marker Score: 476
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 1.29
    Marker Score: 1487
  • Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
    Fold Change: 1.28
    Marker Score: 1857
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 1.27
    Marker Score: 18953
  • Cell Name: stem cell (CL0000034)
    Fold Change: 1.24
    Marker Score: 2952
  • Cell Name: erythroid progenitor cell (CL0000038)
    Fold Change: 1.21
    Marker Score: 1261
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 1.1
    Marker Score: 328
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: 1.05
    Marker Score: 1985.5
  • Cell Name: parietal cell (CL0000162)
    Fold Change: 1.02
    Marker Score: 285
  • Cell Name: paneth cell of colon (CL0009009)
    Fold Change: 1.02
    Marker Score: 293
  • Cell Name: precursor cell (CL0011115)
    Fold Change: 1.01
    Marker Score: 245
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71774
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 1
    Marker Score: 47999
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30402
  • Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
    Fold Change: 0.97
    Marker Score: 407
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.95
    Marker Score: 492
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.95
    Marker Score: 2409
  • Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
    Fold Change: 0.94
    Marker Score: 446
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.94
    Marker Score: 5344
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.91
    Marker Score: 2737
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 0.9
    Marker Score: 14478
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.9
    Marker Score: 360
  • Cell Name: intestine goblet cell (CL0019031)
    Fold Change: 0.89
    Marker Score: 853
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: 0.89
    Marker Score: 2533
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.87
    Marker Score: 314
  • Cell Name: kidney cell (CL1000497)
    Fold Change: 0.87
    Marker Score: 582
  • Cell Name: NKp44-positive group 3 innate lymphoid cell, human (CL0001079)
    Fold Change: 0.87
    Marker Score: 197
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5267
  • Cell Name: stem cell of epidermis (CL1000428)
    Fold Change: 0.85
    Marker Score: 289
  • Cell Name: nephron tubule epithelial cell (CL1000494)
    Fold Change: 0.85
    Marker Score: 200
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 0.85
    Marker Score: 657
  • Cell Name: epithelial cell of esophagus (CL0002252)
    Fold Change: 0.84
    Marker Score: 7235
  • Cell Name: type G enteroendocrine cell (CL0000508)
    Fold Change: 0.84
    Marker Score: 289
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.81
    Marker Score: 12654
  • Cell Name: early T lineage precursor (CL0002425)
    Fold Change: 0.8
    Marker Score: 610
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.78
    Marker Score: 1269
  • Cell Name: alveolar macrophage (CL0000583)
    Fold Change: 0.76
    Marker Score: 19494.5
  • Cell Name: epithelial cell of alveolus of lung (CL0010003)
    Fold Change: 0.74
    Marker Score: 334
  • Cell Name: Cajal-Retzius cell (CL0000695)
    Fold Change: 0.74
    Marker Score: 382
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.73
    Marker Score: 3078
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: 0.71
    Marker Score: 454
  • Cell Name: M cell of gut (CL0000682)
    Fold Change: 0.71
    Marker Score: 184
  • Cell Name: promonocyte (CL0000559)
    Fold Change: 0.71
    Marker Score: 455
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 0.71
    Marker Score: 716
  • Cell Name: brush cell (CL0002204)
    Fold Change: 0.7
    Marker Score: 643
  • Cell Name: P/D1 enteroendocrine cell (CL0002268)
    Fold Change: 0.7
    Marker Score: 262
  • Cell Name: rod bipolar cell (CL0000751)
    Fold Change: 0.68
    Marker Score: 354
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: 0.68
    Marker Score: 173
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 0.67
    Marker Score: 251
  • Cell Name: enteroendocrine cell (CL0000164)
    Fold Change: 0.66
    Marker Score: 344
  • Cell Name: vasa recta ascending limb cell (CL1001131)
    Fold Change: 0.66
    Marker Score: 174
  • Cell Name: pulmonary interstitial fibroblast (CL0002241)
    Fold Change: 0.66
    Marker Score: 526
  • Cell Name: GABAergic amacrine cell (CL4030027)
    Fold Change: 0.65
    Marker Score: 1327
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: 0.64
    Marker Score: 295
  • Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
    Fold Change: 0.64
    Marker Score: 1500
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.64
    Marker Score: 186
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: 0.64
    Marker Score: 673
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: 0.63
    Marker Score: 1577
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: 0.63
    Marker Score: 331
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: 0.62
    Marker Score: 4830.5
  • Cell Name: myeloid cell (CL0000763)
    Fold Change: 0.61
    Marker Score: 978
  • Cell Name: IgA plasma cell (CL0000987)
    Fold Change: 0.61
    Marker Score: 518
  • Cell Name: duct epithelial cell (CL0000068)
    Fold Change: 0.6
    Marker Score: 282
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.6
    Marker Score: 2301
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 0.59
    Marker Score: 634
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 0.59
    Marker Score: 2532
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 0.58
    Marker Score: 12459
  • Cell Name: kidney capillary endothelial cell (CL1000892)
    Fold Change: 0.58
    Marker Score: 182
  • Cell Name: capillary endothelial cell (CL0002144)
    Fold Change: 0.58
    Marker Score: 620

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Other Information

**Key characteristics:** * Gene symbol: CA2 * Ensembl ID: ENSG00000104267 * Protein name: CAH2_HUMAN * Molecular weight: 150 kDa * Chromosome: 17p13.3 * Exon number: 3 **Pathways and functions:** * The CA2 gene is involved in multiple pathways and functions: * Angiotensin-activated signaling pathway: CA2 is a key enzyme that regulates blood pressure and fluid balance by controlling the production of angiotensin II, a potent vasoconstrictor. * Arylesterase activity: CA2 is involved in the metabolism of aromatic compounds, such as phenylalanine and tyramine. * Carbonate dehydratase activity: CA2 is involved in the deamination of carbonate to form bicarbonate, which is essential for the acid-base balance of the body. * Carbon dioxide transport: CA2 is involved in the transport of carbon dioxide in the blood, where it is taken up by red blood cells and transported to the lungs for exhalation. * Cyanamide hydratase activity: CA2 is involved in the metabolism of cyano compounds, such as nitric oxide and nitric acid. * Erythrocytes take up carbon dioxide and release oxygen, Erythrocytes take up oxygen and release carbon dioxide: CA2 is essential for the transport of carbon dioxide in red blood cells. * Metabolism: CA2 is involved in various metabolic processes, including the metabolism of amino acids, lipids, and carbohydrates. * Morphogenesis of an epithelium: CA2 is involved in the morphogenesis of epithelial cells, contributing to the development and maintenance of tissues and organs. * O2/co2 exchange in erythrocytes: CA2 is involved in the oxygenation of red blood cells, where it facilitates the transfer of oxygen from the lungs to the tissues. **Clinical significance:** * Mutations in the CA2 gene have been linked to several human diseases, including hypertension, heart failure, and stroke. * CA2 inhibitors are being investigated as potential therapeutic agents for these diseases. * Studies of CA2 function have also been used to understand the role of carbon dioxide transport and metabolism in various physiological and pathological conditions.

Genular Protein ID: 724538490

Symbol: CAH2_HUMAN

Name: Carbonic anhydrase 2

UniProtKB Accession Codes:

P00918 B2R7G8 Q6FI12 Q96ET9

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BRENDA 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CDD 1 CPTAC 2 CTD 1 ChEBI 12 ChEMBL 1 ChiTaRS 1 DNASU 1 DisGeNET 1 DrugBank 100 DrugCentral 1 EC 2 EMBL 15 EPD 1 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 22 Gene3D 1 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MIM 3 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 100 PDBsum 100 PIR 1 PRO 1 PROSITE 2 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 REPRODUCTION-2DPAGE 2 RNAct 1 Reactome 3 RefSeq 1 Rhea 2 SABIO-RK 1 SMART 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 TreeFam 1 UCD-2DPAGE 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 3108857

Title: Nucleotide sequence of human liver carbonic anhydrase II cDNA.

PubMed ID: 3108857

DOI: 10.1093/nar/15.11.4687

PubMed ID: 3121496

Title: Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II.

PubMed ID: 3121496

DOI: 10.1016/0888-7543(87)90008-5

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 4207120

Title: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.

PubMed ID: 4207120

DOI: 10.1016/s0021-9258(19)42734-8

PubMed ID: 823150

Title: Primary structure of human carbonic anhydrase C.

PubMed ID: 823150

DOI: 10.1016/s0021-9258(17)33081-8

PubMed ID: 3000449

Title: Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements.

PubMed ID: 3000449

DOI: 10.1016/0167-4781(85)90006-5

PubMed ID: 14567693

Title: Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter.

PubMed ID: 14567693

DOI: 10.1021/bi0353124

PubMed ID: 14736710

Title: Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA.

PubMed ID: 14736710

DOI: 10.1152/ajpcell.00382.2003

PubMed ID: 15218065

Title: Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells.

PubMed ID: 15218065

DOI: 10.1113/jphysiol.2004.065110

PubMed ID: 15990874

Title: Metabolon disruption: a mechanism that regulates bicarbonate transport.

PubMed ID: 15990874

DOI: 10.1038/sj.emboj.7600736

PubMed ID: 17314045

Title: Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I.

PubMed ID: 17314045

DOI: 10.1016/j.bmcl.2007.01.113

PubMed ID: 18618712

Title: Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide.

PubMed ID: 18618712

DOI: 10.1002/prot.22144

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 4621826

Title: Crystal structure of human carbonic anhydrase C.

PubMed ID: 4621826

DOI: 10.1038/newbio235131a0

PubMed ID: 3151019

Title: Refined structure of human carbonic anhydrase II at 2.0-A resolution.

PubMed ID: 3151019

DOI: 10.1002/prot.340040406

PubMed ID: 3151020

Title: Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high pH.

PubMed ID: 3151020

DOI: 10.1002/prot.340040407

PubMed ID: 1909891

Title: Conformational mobility of His-64 in the Thr-200TO: human carbonic anhydrase II.

PubMed ID: 1909891

DOI: 10.1021/bi00102a005

PubMed ID: 1932029

Title: Engineering the hydrophobic pocket of carbonic anhydrase II.

PubMed ID: 1932029

DOI: 10.1021/bi00110a008

PubMed ID: 1910042

Title: Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121.

PubMed ID: 1910042

DOI: 10.1016/s0021-9258(19)47376-6

PubMed ID: 1336460

Title: Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions.

PubMed ID: 1336460

DOI: 10.1111/j.1432-1033.1992.tb17490.x

PubMed ID: 1433293

Title: Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.

PubMed ID: 1433293

DOI: 10.1016/0022-2836(92)90531-n

PubMed ID: 1474587

Title: Structure of cobalt carbonic anhydrase complexed with bicarbonate.

PubMed ID: 1474587

DOI: 10.1016/0022-2836(92)90327-g

PubMed ID: 8431430

Title: Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form.

PubMed ID: 8431430

DOI: 10.1021/bi00057a015

PubMed ID: 8485129

Title: Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II.

PubMed ID: 8485129

DOI: 10.1021/bi00068a005

PubMed ID: 8399159

Title: Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II.

PubMed ID: 8399159

DOI: 10.1021/bi00089a005

PubMed ID: 8218160

Title: Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant.

PubMed ID: 8218160

DOI: 10.1021/bi00092a003

PubMed ID: 8482389

Title: The structure of human carbonic anhydrase II in complex with bromide and azide.

PubMed ID: 8482389

DOI: 10.1016/0014-5793(93)81565-h

PubMed ID: 8262987

Title: Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.

PubMed ID: 8262987

DOI: 10.1016/s0021-9258(19)74269-0

PubMed ID: 8331673

Title: Crystal structure of the complex between human carbonic anhydrase II and the aromatic inhibitor 1,2,4-triazole.

PubMed ID: 8331673

DOI: 10.1006/jmbi.1993.1365

PubMed ID: 8451242

Title: Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.

PubMed ID: 8451242

DOI: 10.1002/prot.340150110

PubMed ID: 7901850

Title: Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II.

PubMed ID: 7901850

DOI: 10.1002/prot.340170112

PubMed ID: 15299481

Title: X-ray analysis of metal-substituted human carbonic anhydrase II derivatives.

PubMed ID: 15299481

DOI: 10.1107/s0907444993008790

PubMed ID: 15299482

Title: Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.

PubMed ID: 15299482

DOI: 10.1107/s0907444993009667

PubMed ID: 7803386

Title: Structural consequences of redesigning a protein-zinc binding site.

PubMed ID: 7803386

DOI: 10.1021/bi00255a004

PubMed ID: 8070585

Title: The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide.

PubMed ID: 8070585

DOI: 10.1016/0014-5793(94)00798-5

PubMed ID: 8142888

Title: Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors.

PubMed ID: 8142888

DOI: 10.1002/pro.5560030115

PubMed ID: 7696263

Title: Structural basis of inhibitor affinity to variants of human carbonic anhydrase II.

PubMed ID: 7696263

DOI: 10.1021/bi00012a016

PubMed ID: 7608893

Title: Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants.

PubMed ID: 7608893

DOI: 10.1021/jm00013a004

PubMed ID: 7761440

Title: Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity.

PubMed ID: 7761440

DOI: 10.1073/pnas.92.11.5017

PubMed ID: 8639494

Title: Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II.

PubMed ID: 8639494

DOI: 10.1021/bi9526692

PubMed ID: 8987974

Title: X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.

PubMed ID: 8987974

DOI: 10.1021/bi9617872

PubMed ID: 8557623

Title: Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Implications for the development of a zinc biosensor.

PubMed ID: 8557623

DOI: 10.1074/jbc.271.2.1003

PubMed ID: 9265618

Title: Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine.

PubMed ID: 9265618

DOI: 10.1021/bi970760v

PubMed ID: 9398308

Title: Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity.

PubMed ID: 9398308

DOI: 10.1021/bi971296x

PubMed ID: 9541386

Title: Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination.

PubMed ID: 9541386

DOI: 10.1002/pro.5560070303

PubMed ID: 9865942

Title: Structural analysis of inhibitor binding to human carbonic anhydrase II.

PubMed ID: 9865942

DOI: 10.1002/pro.5560071201

PubMed ID: 10550681

Title: Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?

PubMed ID: 10550681

DOI: 10.1007/s007750050375

PubMed ID: 11015219

Title: Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction.

PubMed ID: 11015219

DOI: 10.1021/bi000937c

PubMed ID: 11076507

Title: Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II.

PubMed ID: 11076507

DOI: 10.1021/bi001649j

PubMed ID: 11327835

Title: Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II.

PubMed ID: 11327835

DOI: 10.1021/bi002295z

PubMed ID: 11572683

Title: Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II.

PubMed ID: 11572683

DOI: 10.1021/ja011034p

PubMed ID: 11802772

Title: Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate.

PubMed ID: 11802772

DOI: 10.1042/0264-6021:3610437

PubMed ID: 12056894

Title: Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant.

PubMed ID: 12056894

DOI: 10.1021/bi020053o

PubMed ID: 12171926

Title: Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase.

PubMed ID: 12171926

DOI: 10.1074/jbc.m205791200

PubMed ID: 11831900

Title: Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV.

PubMed ID: 11831900

DOI: 10.1021/jm010163d

PubMed ID: 12166932

Title: Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation.

PubMed ID: 12166932

DOI: 10.1021/jm011112j

PubMed ID: 11818565

Title: Combinatorial computational method gives new picomolar ligands for a known enzyme.

PubMed ID: 11818565

DOI: 10.1073/pnas.032673399

PubMed ID: 12499545

Title: The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer.

PubMed ID: 12499545

DOI: 10.1107/s0907444902019455

PubMed ID: 14736236

Title: Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition.

PubMed ID: 14736236

DOI: 10.1021/jm030912m

PubMed ID: 15453828

Title: Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent.

PubMed ID: 15453828

DOI: 10.1042/bj20041037

PubMed ID: 15667203

Title: Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II.

PubMed ID: 15667203

DOI: 10.1021/bi0480279

PubMed ID: 15865431

Title: First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors.

PubMed ID: 15865431

DOI: 10.1021/bi047692e

PubMed ID: 16214338

Title: 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.

PubMed ID: 16214338

DOI: 10.1016/j.bmcl.2005.08.069

PubMed ID: 16134940

Title: Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II.

PubMed ID: 16134940

DOI: 10.1021/jm050333c

PubMed ID: 16106378

Title: Proton transfer in a Thr200His mutant of human carbonic anhydrase II.

PubMed ID: 16106378

DOI: 10.1002/prot.20615

PubMed ID: 16511248

Title: Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II.

PubMed ID: 16511248

DOI: 10.1107/s1744309105038248

PubMed ID: 16820676

Title: X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes.

PubMed ID: 16820676

DOI: 10.1107/s1744309106020446

PubMed ID: 16290146

Title: Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib.

PubMed ID: 16290146

DOI: 10.1016/j.bmcl.2005.09.040

PubMed ID: 16759856

Title: N-hydroxyurea -- a versatile zinc binding function in the design of metalloenzyme inhibitors.

PubMed ID: 16759856

DOI: 10.1016/j.bmcl.2006.05.068

PubMed ID: 17000110

Title: Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform II.

PubMed ID: 17000110

DOI: 10.1016/j.bmcl.2006.09.022

PubMed ID: 16807956

Title: Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme.

PubMed ID: 16807956

DOI: 10.1002/chem.200600159

PubMed ID: 16506782

Title: Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity.

PubMed ID: 16506782

DOI: 10.1021/ja057257n

PubMed ID: 16787097

Title: Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the interaction of a fluorescent antitumor sulfonamide with isozyme II and IX.

PubMed ID: 16787097

DOI: 10.1021/ja061574s

PubMed ID: 16686544

Title: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design.

PubMed ID: 16686544

DOI: 10.1021/jm0603320

PubMed ID: 16942027

Title: Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX.

PubMed ID: 16942027

DOI: 10.1021/jm060531j

PubMed ID: 17125255

Title: Carbonic anhydrase inhibitors: clash with Ala65 as a means for designing inhibitors with low affinity for the ubiquitous isozyme II, exemplified by the crystal structure of the topiramate sulfamide analogue.

PubMed ID: 17125255

DOI: 10.1021/jm060807n

PubMed ID: 17181151

Title: 2-substituted estradiol bis-sulfamates, multitargeted antitumor agents: synthesis, in vitro SAR, protein crystallography, and in vivo activity.

PubMed ID: 17181151

DOI: 10.1021/jm060705x

PubMed ID: 17705204

Title: Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste.

PubMed ID: 17705204

DOI: 10.1002/anie.200701189

PubMed ID: 17319692

Title: Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism.

PubMed ID: 17319692

DOI: 10.1021/bi062066y

PubMed ID: 17330962

Title: 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.

PubMed ID: 17330962

DOI: 10.1021/bi602620k

PubMed ID: 17127057

Title: Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.

PubMed ID: 17127057

DOI: 10.1016/j.bmcl.2006.11.027

PubMed ID: 17251017

Title: 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.

PubMed ID: 17251017

DOI: 10.1016/j.bmcl.2006.12.099

PubMed ID: 17346964

Title: 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.

PubMed ID: 17346964

DOI: 10.1016/j.bmcl.2007.02.068

PubMed ID: 17540563

Title: Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides -- solution and crystallographic studies.

PubMed ID: 17540563

DOI: 10.1016/j.bmcl.2007.05.045

PubMed ID: 17588751

Title: Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies.

PubMed ID: 17588751

DOI: 10.1016/j.bmcl.2007.06.044

PubMed ID: 17071654

Title: Location of binding sites in small molecule rescue of human carbonic anhydrase II.

PubMed ID: 17071654

DOI: 10.1529/biophysj.106.093203

PubMed ID: 17407288

Title: Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II.

PubMed ID: 17407288

DOI: 10.1021/ja068359w

PubMed ID: 18266323

Title: Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and structural study.

PubMed ID: 18266323

DOI: 10.1021/bi702385k

PubMed ID: 18942852

Title: Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.

PubMed ID: 18942852

DOI: 10.1021/bi801473w

PubMed ID: 18024029

Title: Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies.

PubMed ID: 18024029

DOI: 10.1016/j.bmcl.2007.10.110

PubMed ID: 18162396

Title: Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies.

PubMed ID: 18162396

DOI: 10.1016/j.bmcl.2007.12.022

PubMed ID: 18374572

Title: Carbonic anhydrase inhibitors. Interaction of indapamide and related diuretics with 12 mammalian isozymes and X-ray crystallographic studies for the indapamide-isozyme II adduct.

PubMed ID: 18374572

DOI: 10.1016/j.bmcl.2008.03.051

PubMed ID: 18359629

Title: Carbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of thr200 and gln92 for obtaining tight-binding inhibitors.

PubMed ID: 18359629

DOI: 10.1016/j.bmcl.2008.03.023

PubMed ID: 18640037

Title: Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray crystallographic studies.

PubMed ID: 18640037

DOI: 10.1016/j.bmcl.2008.06.105

PubMed ID: 18161740

Title: Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform II.

PubMed ID: 18161740

DOI: 10.1002/cmdc.200700274

PubMed ID: 18461940

Title: Structure of a (129)Xe-cryptophane biosensor complexed with human carbonic anhydrase II.

PubMed ID: 18461940

DOI: 10.1021/ja802214x

PubMed ID: 18768466

Title: Entrapment of carbon dioxide in the active site of carbonic anhydrase II.

PubMed ID: 18768466

DOI: 10.1074/jbc.m805353200

PubMed ID: 18260615

Title: Structure-activity relationships of C-17 cyano-substituted estratrienes as anticancer agents.

PubMed ID: 18260615

DOI: 10.1021/jm701319c

Sequence Information:

  • Length: 260
  • Mass: 29246
  • Checksum: 2EC2BB7548F10558
  • Sequence:
    • MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL 
NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL 
VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP 
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM 
VDNWRPAQPL KNRQIKASFK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.