Details for: CA2

Gene ID: 760

Symbol: CA2

Ensembl ID: ENSG00000104267

Description: carbonic anhydrase 2

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 71.0052
    Cell Significance Index: -18.0100
  • Cell Name: basophilic erythroblast (CL0000549)
    Fold Change: 69.6082
    Cell Significance Index: 31.7000
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 50.2977
    Cell Significance Index: -20.7200
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 41.9724
    Cell Significance Index: -21.5900
  • Cell Name: columnar/cuboidal epithelial cell (CL0000075)
    Fold Change: 13.2267
    Cell Significance Index: 50.6500
  • Cell Name: kidney collecting duct cell (CL1001225)
    Fold Change: 4.8287
    Cell Significance Index: 16.5800
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 4.7769
    Cell Significance Index: -18.8500
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 4.2319
    Cell Significance Index: 197.3100
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 4.0963
    Cell Significance Index: 185.6700
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 3.6639
    Cell Significance Index: -9.8200
  • Cell Name: epithelial cell of pancreas (CL0000083)
    Fold Change: 3.3152
    Cell Significance Index: 54.6300
  • Cell Name: oral mucosa squamous cell (CL1001576)
    Fold Change: 2.9501
    Cell Significance Index: 25.3500
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: 2.7002
    Cell Significance Index: 58.5000
  • Cell Name: kidney cell (CL1000497)
    Fold Change: 2.0591
    Cell Significance Index: 16.4400
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: 1.9086
    Cell Significance Index: 217.8700
  • Cell Name: paneth cell of colon (CL0009009)
    Fold Change: 1.3074
    Cell Significance Index: 19.5900
  • Cell Name: extravillous trophoblast (CL0008036)
    Fold Change: 1.2827
    Cell Significance Index: 7.9700
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: 1.0588
    Cell Significance Index: 66.7300
  • Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
    Fold Change: 0.8157
    Cell Significance Index: 5.0200
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: 0.7995
    Cell Significance Index: 9.5300
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 0.6679
    Cell Significance Index: 49.7800
  • Cell Name: glomerular capillary endothelial cell (CL1001005)
    Fold Change: 0.5286
    Cell Significance Index: 1.9700
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 0.5193
    Cell Significance Index: 24.4100
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.4869
    Cell Significance Index: 52.9700
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: 0.4736
    Cell Significance Index: 15.1700
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.4382
    Cell Significance Index: 12.6300
  • Cell Name: seromucus secreting cell (CL0000159)
    Fold Change: 0.3697
    Cell Significance Index: 7.7100
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 0.3662
    Cell Significance Index: 25.9000
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 0.3508
    Cell Significance Index: 18.4200
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: 0.2910
    Cell Significance Index: 47.3300
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 0.2815
    Cell Significance Index: 19.4700
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: 0.2379
    Cell Significance Index: 27.2600
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.2239
    Cell Significance Index: 42.6200
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 0.2234
    Cell Significance Index: 28.8600
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.1959
    Cell Significance Index: 176.8700
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.1925
    Cell Significance Index: 19.0400
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.1667
    Cell Significance Index: 59.8000
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.1523
    Cell Significance Index: 19.5200
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.1306
    Cell Significance Index: 98.8200
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 0.0866
    Cell Significance Index: 1.8700
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.0602
    Cell Significance Index: 38.2500
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: 0.0436
    Cell Significance Index: 1.0900
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: 0.0244
    Cell Significance Index: 17.9100
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.0205
    Cell Significance Index: 9.0700
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.0196
    Cell Significance Index: 3.8800
  • Cell Name: fallopian tube secretory epithelial cell (CL4030006)
    Fold Change: 0.0181
    Cell Significance Index: 0.2800
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.0031
    Cell Significance Index: 1.7200
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.0007
    Cell Significance Index: 0.1300
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0059
    Cell Significance Index: -11.1900
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: -0.0080
    Cell Significance Index: -0.2800
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0089
    Cell Significance Index: -6.5900
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0106
    Cell Significance Index: -6.6200
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0116
    Cell Significance Index: -21.3600
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0134
    Cell Significance Index: -20.6900
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0154
    Cell Significance Index: -20.9400
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: -0.0189
    Cell Significance Index: -13.0600
  • Cell Name: endothelial cell of placenta (CL0009092)
    Fold Change: -0.0199
    Cell Significance Index: -0.1200
  • Cell Name: Mueller cell (CL0000636)
    Fold Change: -0.0208
    Cell Significance Index: -0.1600
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0208
    Cell Significance Index: -11.7100
  • Cell Name: intrahepatic cholangiocyte (CL0002538)
    Fold Change: -0.0212
    Cell Significance Index: -0.0800
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: -0.0217
    Cell Significance Index: -3.7100
  • Cell Name: proerythroblast (CL0000547)
    Fold Change: -0.0248
    Cell Significance Index: -0.3600
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0284
    Cell Significance Index: -12.9100
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0375
    Cell Significance Index: -3.8300
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.0420
    Cell Significance Index: -12.0900
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.0444
    Cell Significance Index: -2.4900
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.0470
    Cell Significance Index: -5.4800
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: -0.0499
    Cell Significance Index: -10.0100
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -0.0549
    Cell Significance Index: -1.1700
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0579
    Cell Significance Index: -8.4100
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.0664
    Cell Significance Index: -4.0800
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.0725
    Cell Significance Index: -15.2800
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.0965
    Cell Significance Index: -7.6400
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -0.0989
    Cell Significance Index: -2.6400
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.1009
    Cell Significance Index: -2.8200
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: -0.1113
    Cell Significance Index: -13.6900
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: -0.1163
    Cell Significance Index: -15.9700
  • Cell Name: neuron associated cell (CL0000095)
    Fold Change: -0.1337
    Cell Significance Index: -5.4800
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: -0.1342
    Cell Significance Index: -6.9900
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -0.1471
    Cell Significance Index: -11.2900
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: -0.1615
    Cell Significance Index: -8.3900
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.1789
    Cell Significance Index: -18.6300
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: -0.1813
    Cell Significance Index: -21.3800
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -0.1915
    Cell Significance Index: -9.6800
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: -0.2052
    Cell Significance Index: -2.2000
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.2074
    Cell Significance Index: -12.7200
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.2510
    Cell Significance Index: -16.8800
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: -0.2627
    Cell Significance Index: -7.0400
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: -0.2806
    Cell Significance Index: -2.9100
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: -0.3035
    Cell Significance Index: -2.3200
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: -0.3181
    Cell Significance Index: -4.8400
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: -0.3346
    Cell Significance Index: -21.5900
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: -0.3512
    Cell Significance Index: -9.5600
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -0.3708
    Cell Significance Index: -9.9200
  • Cell Name: stratified epithelial cell (CL0000079)
    Fold Change: -0.3781
    Cell Significance Index: -13.8800
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: -0.3918
    Cell Significance Index: -6.6000
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: -0.3934
    Cell Significance Index: -8.1600
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.4011
    Cell Significance Index: -17.7400
  • Cell Name: foveolar cell of stomach (CL0002179)
    Fold Change: -0.4126
    Cell Significance Index: -2.6900
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: -0.4176
    Cell Significance Index: -12.3000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** CA2 is a zinc-dependent enzyme that catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of oxygen and carbon dioxide in erythrocytes. It is a tetrameric enzyme composed of four subunits, each with a unique amino acid sequence. CA2 exhibits high affinity for CO2 and H+ ions, allowing it to efficiently catalyze the hydration reaction. This enzyme is also capable of binding to other molecules, including chloride, zinc, and dipeptides, which modulate its activity. **Pathways and Functions:** CA2 is involved in various cellular pathways, including: 1. **Angiotensin-activated signaling pathway:** CA2 is activated by angiotensin II, a potent vasoconstrictor, and plays a role in regulating blood pressure and electrolyte balance. 2. **Apical part of cell:** CA2 is localized to the apical membrane of cells, where it facilitates the exchange of oxygen and carbon dioxide. 3. **Metabolism:** CA2 is involved in the regulation of metabolic pathways, including glycolysis, gluconeogenesis, and the citric acid cycle. 4. **Morphogenesis of an epithelium:** CA2 plays a role in the development and maintenance of epithelial tissues, including the stomach and colon. 5. **Neuron cellular homeostasis:** CA2 is involved in regulating synaptic transmission and neuronal function. **Clinical Significance:** CA2 has been implicated in various diseases, including: 1. **Erythrocyte disorders:** Mutations in the CA2 gene can lead to erythrocyte disorders, such as carbonic anhydrase deficiency, which affects the ability of erythrocytes to transport oxygen and carbon dioxide. 2. **Renal diseases:** CA2 is involved in the regulation of electrolyte balance and blood pressure in the kidneys, making it a potential target for treating renal diseases, such as hypertension and kidney failure. 3. **Cancer:** CA2 has been overexpressed in various types of cancer, including breast, lung, and colon cancer, suggesting its potential role in tumorigenesis. 4. **Neurological disorders:** CA2 has been implicated in the pathogenesis of neurological disorders, such as Alzheimer's disease and Parkinson's disease. In conclusion, CA2 is a vital enzyme that plays a crucial role in maintaining cellular homeostasis and facilitating the exchange of oxygen and carbon dioxide in erythrocytes. Its involvement in various cellular pathways and its clinical significance in diseases make it an important target for further research and therapeutic intervention.

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 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 22 Gene3D 1 GeneCards 1 GeneTree 1 GeneWiki 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 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 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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.