Carbonic anhydrase II
CA2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| |||||||||||||||||||||||||||||||||||||||||||||||||||
Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | CA2, CA-II, CAC, CAII, Car2, HEL-76, HEL-S-282, Carbonic anhydrase II, carbonic anhydrase 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 611492; MGI: 88269; HomoloGene: 37256; GeneCards: CA2; OMA:CA2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
|
Carbonic anhydrase II (gene name CA2) is one of sixteen forms of human α carbonic anhydrases.[5] Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. [6] Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis.[7]
Interactions
Carbonic anhydrase II has been shown to interact with band 3[8][9][10][11] and sodium-hydrogen antiporter 1.[12]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000104267 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027562 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Frost, S., & McKenna, R. (2014). Carbonic anhydrase : Mechanism, regulation, links to disease, and industrial applications(Subcellular biochemistry). Dordrecht: Springer. doi:10.1007/978-94-007-7359-2
- ^ "Entrez Gene: CA2 carbonic anhydrase II".
- ^ Reference, Genetics Home. "Osteopetrosis". Genetics Home Reference. Retrieved 2018-10-31.
- ^ Sterling, D; Reithmeier R A; Casey J R (December 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51). United States: 47886–94. doi:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
- ^ Vince, J W; Reithmeier R A (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43). UNITED STATES: 28430–7. doi:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
- ^ Vince, J W; Carlsson U; Reithmeier R A (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44). UNITED STATES: 13344–9. doi:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
- ^ Vince, J W; Reithmeier R A (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18). UNITED STATES: 5527–33. doi:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
- ^ Li, Xiuju; Alvarez Bernardo; Casey Joseph R; Reithmeier Reinhart A F; Fliegel Larry (September 2002). "Carbonic anhydrase II binds to and enhances activity of the Na+/H+ exchanger". J. Biol. Chem. 277 (39). United States: 36085–91. doi:10.1074/jbc.M111952200. ISSN 0021-9258. PMID 12138085.
Further reading
- Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annu. Rev. Biochem. 64 (1): 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
- Kumpulainen T (1979). "Immunohistochemical localization of human carbonic anhydrase isoenzyme C.". Histochemistry. 62 (3): 271–80. doi:10.1007/BF00508355. PMID 114507. S2CID 21606492.
- Henderson LE, Henriksson D, Nyman PO (1976). "Primary structure of human carbonic anhydrase C." J. Biol. Chem. 251 (18): 5457–63. doi:10.1016/S0021-9258(17)33081-8. PMID 823150.
- Hu PY, Roth DE, Skaggs LA, et al. (1993). "A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries". Hum. Mutat. 1 (4): 288–92. doi:10.1002/humu.1380010404. PMID 1301935. S2CID 28188859.
- Roth DE, Venta PJ, Tashian RE, Sly WS (1992). "Molecular basis of human carbonic anhydrase II deficiency". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1804–8. Bibcode:1992PNAS...89.1804R. doi:10.1073/pnas.89.5.1804. PMC 48541. PMID 1542674.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Schwartz GJ, Brion LP, Corey HE, Dorfman HD (1991). "Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification)". Skeletal Radiol. 20 (6): 447–52. doi:10.1007/BF00191090. PMID 1925679. S2CID 29176430.
- Venta PJ, Welty RJ, Johnson TM, et al. (1991). "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene". Am. J. Hum. Genet. 49 (5): 1082–90. PMC 1683243. PMID 1928091.
- Venta PJ, Tashian RE (1990). "PCR detection of the TAQ1 polymorphism at the CA2 locus". Nucleic Acids Res. 18 (18): 5585. doi:10.1093/nar/18.18.5585. PMC 332284. PMID 1977133.
- Sato S, Zhu XL, Sly WS (1990). "Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients". Proc. Natl. Acad. Sci. U.S.A. 87 (16): 6073–6. Bibcode:1990PNAS...87.6073S. doi:10.1073/pnas.87.16.6073. PMC 54474. PMID 2117271.
- Kaunisto K, Parkkila S, Tammela T, et al. (1990). "Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract". Histochemistry. 94 (4): 381–6. doi:10.1007/BF00266444. PMID 2121671. S2CID 22668787.
- Backman U, Danielsson B, Wistrand PJ (1991). "The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease". Scand. J. Clin. Lab. Invest. 50 (6): 627–33. doi:10.3109/00365519009089180. PMID 2123360.
- Forsman C, Behravan G, Osterman A, Jonsson BH (1989). "Production of active human carbonic anhydrase II in E. coli". Acta Chemica Scandinavica B. 42 (5): 314–8. doi:10.3891/acta.chem.scand.42b-0314. PMID 2850697.
- Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE (1986). "Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements" (PDF). Biochim. Biophys. Acta. 826 (4): 195–201. doi:10.1016/0167-4781(85)90006-5. hdl:2027.42/25466. PMID 3000449.
- Ohlsson A, Cumming WA, Paul A, Sly WS (1986). "Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification". Pediatrics. 77 (3): 371–81. doi:10.1542/peds.77.3.371. PMID 3081869. S2CID 33477826.
- Nakai H, Byers MG, Venta PJ, et al. (1987). "The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22". Cytogenet. Cell Genet. 44 (4): 234–5. doi:10.1159/000132378. PMID 3107918.
- Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D (1987). "Nucleotide sequence of human liver carbonic anhydrase II cDNA". Nucleic Acids Res. 15 (11): 4687. doi:10.1093/nar/15.11.4687. PMC 340889. PMID 3108857.
- Murakami H, Marelich GP, Grubb JH, et al. (1988). "Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II". Genomics. 1 (2): 159–66. doi:10.1016/0888-7543(87)90008-5. PMID 3121496.
- Eriksson AE, Jones TA, Liljas A (1989). "Refined structure of human carbonic anhydrase II at 2.0 A resolution". Proteins. 4 (4): 274–82. doi:10.1002/prot.340040406. PMID 3151019. S2CID 25590322.
- Eriksson AE, Kylsten PM, Jones TA, Liljas A (1989). "Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH". Proteins. 4 (4): 283–93. doi:10.1002/prot.340040407. PMID 3151020. S2CID 25849532.
- v
- t
- e
- 12ca: ALTERING THE MOUTH OF A HYDROPHOBIC POCKET. STRUCTURE AND KINETICS OF HUMAN CARBONIC ANHYDRASE II MUTANTS AT RESIDUE VAL-121
- 1a42: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE
- 1am6: CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE
- 1avn: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE ACTIVATOR
- 1bcd: X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE
- 1bic: CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-
- 1bn1: CARBONIC ANHYDRASE II INHIBITOR
- 1bn3: CARBONIC ANHYDRASE II INHIBITOR
- 1bn4: CARBONIC ANHYDRASE II INHIBITOR
- 1bnm: CARBONIC ANHYDRASE II INHIBITOR
- 1bnn: CARBONIC ANHYDRASE II INHIBITOR
- 1bnq: CARBONIC ANHYDRASE II INHIBITOR
- 1bnt: CARBONIC ANHYDRASE II INHIBITOR
- 1bnu: CARBONIC ANHYDRASE II INHIBITOR
- 1bnv: CARBONIC ANHYDRASE II INHIBITOR
- 1bnw: CARBONIC ANHYDRASE II INHIBITOR
- 1bv3: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA
- 1ca2: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
- 1ca3: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.
- 1cah: STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE
- 1cai: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1caj: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1cak: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1cal: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1cam: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1can: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
- 1cao: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS
- 1cay: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE
- 1caz: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE
- 1ccs: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
- 1cct: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
- 1ccu: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY
- 1cil: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
- 1cim: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
- 1cin: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS
- 1cnb: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES
- 1cnc: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES
- 1cng: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
- 1cnh: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
- 1cni: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
- 1cnj: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
- 1cnk: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE
- 1cnw: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
- 1cnx: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
- 1cny: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS
- 1cra: THE COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND THE AROMATIC INHIBITOR 1,2,4-TRIAZOLE
- 1cva: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1cvb: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II
- 1cvc: REDESIGNING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF A HIS2ASP-ZN2+ METAL COORDINATION POLYHEDRON
- 1cvd: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
- 1cve: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
- 1cvf: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
- 1cvh: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
- 1dca: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH
- 1dcb: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH
- 1eou: CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE
- 1f2w: THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION
- 1fql: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
- 1fqm: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
- 1fqn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
- 1fqr: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
- 1fr4: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT
- 1fr7: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
- 1fsn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
- 1fsq: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
- 1fsr: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT
- 1g0e: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 4-METHYLIMIDAZOLE
- 1g0f: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II
- 1g1d: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE
- 1g3z: CARBONIC ANHYDRASE II (F131V)
- 1g45: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE
- 1g46: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g48: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g4j: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g4o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE
- 1g52: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g53: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g54: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE
- 1g6v: Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase
- 1h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
- 1h9n: H119N CARBONIC ANHYDRASE II
- 1h9q: H119Q CARBONIC ANHYDRASE II
- 1hca: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.
- 1hea: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (E.C.4.2.1.1) MUTANT WITH LEU 198 REPLACED BY ARG (L198R)
- 1heb: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
- 1hec: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
- 1hed: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II
- 1hva: ENGINEERING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF THE HIS-94-> CYS APOENZYME IN A NEW CRYSTALLINE FORM
- 1i8z: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
- 1i90: CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 4-AMINO-3,4-DIHYDRO-2-(3-METHOXYPROPYL)-, 1,1-DIOXIDE, (R)
- 1i91: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE
- 1i9l: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(4-FLUOROPHENYL)METHYL]-BENZAMIDE
- 1i9m: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1i9n: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,5-DIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1i9o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1i9p: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4,6-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1i9q: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(3,4,5-TRIFLUOROPHENYL)METHYL]-BENZAMIDE
- 1if4: Carbonic Anhydrase II Complexed With 4-fluorobenzenesulfonamide
- 1if5: Carbonic Anhydrase II Complexed With 2,6-difluorobenzenesulfonamide
- 1if6: Carbonic Anhydrase II Complexed With 3,5-difluorobenzenesulfonamide
- 1if7: Carbonic Anhydrase II Complexed With (R)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
- 1if8: Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
- 1if9: Carbonic Anhydrase II Complexed With N-[2-(1H-Indol-5-yl)-butyl]-4-sulfamoyl-benzamide
- 1kwq: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 2000-07
- 1kwr: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 0134-36
- 1lg5: Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol
- 1lg6: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Thiocyanate
- 1lgd: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate
- 1lug: Full Matrix Error Analysis of Carbonic Anhydrase
- 1lzv: Site-Specific Mutant (Tyr7 replaced with His) of Human Carbonic Anhydrase II
- 1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution
- 1mua: STRUCTURE AND ENERGETICS OF A NON-PROLINE CIS-PEPTIDYL LINKAGE IN AN ENGINEERED PROTEIN
- 1okl: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR 5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONAMIDE
- 1okm: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR 4-SULFONAMIDE-[1-(4-AMINOBUTANE)]BENZAMIDE
- 1okn: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR 4-SULFONAMIDE-[1-(4-N-(5-FLUORESCEIN THIOUREA)BUTANE)]
- 1oq5: CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR
- 1ray: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE
- 1raz: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE
- 1rza: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
- 1rzb: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
- 1rzc: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
- 1rzd: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
- 1rze: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
- 1t9n: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1tb0: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1tbt: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1te3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1teq: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1teu: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1tg3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1tg9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1th9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1thk: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II
- 1ttm: Human carbonic anhydrase II complexed with 667-coumate
- 1uga: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)
- 1ugb: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY GLY (A65G)
- 1ugc: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)
- 1ugd: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)
- 1uge: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY LEU (A65L)
- 1ugf: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)
- 1ugg: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM
- 1xeg: Crystal structure of human carbonic anhydrase II complexed with an acetate ion
- 1xev: Crystal structure of human carbonic anhydrase II in a new crystal form
- 1xpz: Structure of human carbonic anhydrase II with 4-[4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole
- 1xq0: Structure of human carbonic anhydrase II with 4-[(3-bromo-4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole
- 1yda: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
- 1ydb: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
- 1ydc: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
- 1ydd: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
- 1yo0: Proton Transfer from His200 in Human Carbonic Anhydrase II
- 1yo1: Proton Transfer from His200 in Human Carbonic Anhydrase II
- 1yo2: Proton Transfer from His200 in Human Carbonic Anhydrase II
- 1z9y: carbonic anhydrase II in complex with furosemide as sulfonamide inhibitor
- 1ze8: Carbonic anhydrase II in complex with a membrane-impermeant sulfonamide inhibitor
- 1zfk: carbonic anhydrase II in complex with N-4-sulfonamidphenyl-N'-4-methylbenzosulfonylurease as sulfonamide inhibitor
- 1zfq: carbonic anhydrase II in complex with ethoxzolamidphenole as sulfonamide inhibitor
- 1zge: carbonic anhydrase II in complex with p-Sulfonamido-o,o'-dichloroaniline as sulfonamide inhibitor
- 1zgf: carbonic anhydrase II in complex with trichloromethiazide as sulfonamide inhibitor
- 1zh9: carbonic anhydrase II in complex with N-4-Methyl-1-piperazinyl-N'-(p-sulfonamide)phenylthiourea as sulfonamide inhibitor
- 1zsa: CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
- 1zsb: CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE ANALOGUE ACETAZOLAMIDE
- 1zsc: CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM
- 2abe: 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
- 2aw1: 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
- 2ax2: Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II
- 2ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H
- 2cba: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
- 2cbb: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
- 2cbc: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
- 2cbd: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
- 2cbe: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES
- 2eu2: Human Carbonic Anhydrase II in complex with novel inhibitors
- 2eu3: Human Carbonic anhydrase II in complex with novel inhibitors
- 2ez7: 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
- 2f14: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with a Fluorescent Inhibitor
- 2fmg: 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: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanine
- 2fmz: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.
- 2fnk: Activation of Human Carbonic Anhydrase II by exogenous proton donors
- 2fnm: Activation of human carbonic anhdyrase II by exogenous proton donors
- 2fnn: Activation of human carbonic anhydrase II by exogenous proton donors
- 2foq: Human Carbonic Anhydrase II complexed with two-prong inhibitors
- 2fos: Human Carbonic Anhydrase II complexed with two-prong inhibitors
- 2fou: Human Carbonic Anhydrase II complexed with two-prong inhibitors
- 2fov: Human Carbonic Anhydrase II complexed with two-prong inhibitors
- 2gd8: Crystal structure analysis of the human carbonic anhydrase II in complex with a 2-substituted estradiol bis-sulfamate
- 2geh: N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
- 2h15: Carbonic anhydrase inhibitors: Clashing with Ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme II
- 2h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE
- 2hd6: Crystal structure of the human carbonic anhydrase II in complex with a hypoxia-activatable sulfonamide.
- 2hkk: Carbonic anhydrase activators: Solution and X-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms
- 2hl4: Crystal structure analysis of human carbonic anhydrase II in complex with a benzenesulfonamide derivative
- 2hnc: Crystal structure of the human carbonic anhydrase II in complex with the 5-amino-1,3,4-thiadiazole-2-sulfonamide inhibitor.
- 2hoc: Crystal structure of the human carbonic anhydrase II in complex with the 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide inhibitor
- 2ili: Refine atomic structure of human carbonic anhydrase II
- 2nng: Structure of inhibitor binding to Carbonic Anhydrase II
- 2nno: Structure of inhibitor binding to Carbonic Anhydrase II
- 2nns: Structure of inhibitor binding to Carbonic Anhydrase II
- 2nnv: Structure of inhibitor binding to Carbonic Anhydrase II
- 2nwo: Structural and kinetic effect of hydrophobic mutations in the active site of human carbonic anhydrase II
- 2nwp: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
- 2nwy: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II
- 2nwz: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II
- 2nxr: Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase II
- 2nxs: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
- 2nxt: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II
- 2o4z: Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor
- 3ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H
- 4ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
- 4cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
- 5ca2: CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II
- 5cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION
- 6ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
- 7ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
- 8ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
- 9ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II
This article on a gene on human chromosome 8 is a stub. You can help Wikipedia by expanding it. |
- v
- t
- e