Tmic
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NameCarbonic anhydrase 1
Synonyms
  • 4.2.1.1
  • CA-I
  • CAB
  • Carbonate dehydratase I
  • Carbonic anhydrase B
  • Carbonic anhydrase I
Gene NameCA1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0010047|Carbonic anhydrase 1
MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEI
INVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELH
VAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNF
DPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
Number of residues261
Molecular Weight28870.0
Theoretical pI7.14
GO Classification
Functions
  • zinc ion binding
  • hydro-lyase activity
  • carbonate dehydratase activity
  • arylesterase activity
Processes
  • bicarbonate transport
  • one-carbon metabolic process
  • small molecule metabolic process
Components
  • cytosol
  • extracellular exosome
General FunctionZinc ion binding
Specific FunctionReversible hydration of carbon dioxide. Can hydrates cyanamide to urea.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID29600
UniProtKB IDP00915
UniProtKB Entry NameCAH1_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0010048|Carbonic anhydrase 1 (CA1)
ATGGCAAGTCCAGACTGGGGATATGATGACAAAAATGGTCCTGAACAATGGAGCAAGCTG
TATCCCATTGCCAATGGAAATAACCAGTCCCCTGTTGATATTAAAACCAGTGAAACCAAA
CATGACACCTCTCTGAAACCTATTAGTGTCTCCTACAACCCAGCCACAGCCAAAGAAATT
ATCAATGTGGGGCATTCCTTCCATGTAAATTTTGAGGACAACGATAACCGATCAGTGCTG
AAAGGTGGTCCTTTCTCTGACAGCTACAGGCTCTTTCAGTTCCATTTTCACTGGGGCAGT
ACAAATGAGCATGGTTCAGAACATACAGTGGATGGAGTCAAATATTCTGCCGAGCTTCAC
GTAGCTCACTGGAATTCTGCAAAGTACTCCAGCCTTGCTGAAGCTGCCTCAAAGGCTGAT
GGTTTGGCAGTTATTGGTGTTTTGATGAAGGTTGGTGAGGCCAACCCAAAGCTGCAGAAA
GTACTTGATGCCCTCCAAGCAATTAAAACCAAGGGCAAACGAGCCCCATTCACAAATTTT
GACCCCTCTACTCTCCTTCCTTCATCCCTGGATTTCTGGACCTACCCTGGCTCTCTGACT
CATCCTCCTCTTTATGAGAGTGTAACTTGGATCATCTGTAAGGAGAGCATCAGTGTCAGC
TCAGAGCAGCTGGCACAATTCCGCAGCCTTCTATCAAATGTTGAAGGTGATAACGCTGTC
CCCATGCAGCACAACAACCGCCCAACCCAACCTCTGAAGGGCAGAACAGTGAGAGCTTCA
TTTTGA
GenBank Gene IDX05014
GeneCard IDNot Available
GenAtlas IDCA1
HGNC IDHGNC:1368
Chromosome Location8
Locus8q13-q22.1
References
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  2. Lowe N, Brady HJ, Barlow JH, Sowden JC, Edwards M, Butterworth PH: Structure and methylation patterns of the gene encoding human carbonic anhydrase I. Gene. 1990 Sep 14;93(2):277-83. 2121614
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  4. Giraud N, Marriq C, Laurent-Tabusse G: [Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)]. Biochimie. 1974;56(8):1031-43. 4217196
  5. Andersson B, Nyman PO, Strid L: Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun. 1972 Aug 7;48(3):670-7. 4625868
  6. Lin KT, Deutsch HF: Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J Biol Chem. 1973 Mar 25;248(6):1885-93. 4632246
  7. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. 4207120
  8. Briganti F, Mangani S, Scozzafava A, Vernaglione G, Supuran CT: Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction? J Biol Inorg Chem. 1999 Oct;4(5):528-36. 10550681
  9. Temperini C, Scozzafava A, Vullo D, Supuran CT: 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. Chemistry. 2006 Sep 18;12(27):7057-66. 16807956
  10. Temperini C, Scozzafava A, Vullo D, Supuran CT: 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. J Med Chem. 2006 May 18;49(10):3019-27. 16686544
  11. Temperini C, Innocenti A, Scozzafava A, Mastrolorenzo A, Supuran CT: Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV. Bioorg Med Chem Lett. 2007 Feb 1;17(3):628-35. Epub 2006 Nov 15. 17127057
  12. Crocetti L, Maresca A, Temperini C, Hall RA, Scozzafava A, Muhlschlegel FA, Supuran CT: A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases. Bioorg Med Chem Lett. 2009 Mar 1;19(5):1371-5. doi: 10.1016/j.bmcl.2009.01.038. Epub 2009 Jan 19. 19186056
  13. Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT: Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc. 2009 Mar 4;131(8):3057-62. doi: 10.1021/ja809683v. 19206230
  14. Di Fiore A, Monti SM, Hilvo M, Parkkila S, Romano V, Scaloni A, Pedone C, Scozzafava A, Supuran CT, De Simone G: Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide. Proteins. 2009 Jan;74(1):164-75. doi: 10.1002/prot.22144. 18618712
  15. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
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  17. Kannan KK, Fridborg K, Bergsten PC, Liljas A, Lovgren S, Petef M, Strandberg B, Waara I, Adler L, Falkbring SO, Gothe PO, Nyman PO: Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications. J Mol Biol. 1972 Feb 14;63(3):601-4. 4622589
  18. Kannan KK, Notstrand B, Fridborg K, Lovgren S, Ohlsson A, Petef M: Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution. Proc Natl Acad Sci U S A. 1975 Jan;72(1):51-5. 804171
  19. Kannan KK, Ramanadham M, Jones TA: Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. 6430186
  20. Kumar V, Kannan KK, Sathyamurthi P: Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes. Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):731-8. 15299369
  21. Kumar V, Kannan KK: Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate. J Mol Biol. 1994 Aug 12;241(2):226-32. 8057362
  22. Chakravarty S, Kannan KK: Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme. J Mol Biol. 1994 Oct 21;243(2):298-309. 7932756
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  24. Temperini C, Scozzafava A, Supuran CT: Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I. Bioorg Med Chem Lett. 2006 Oct 1;16(19):5152-6. Epub 2006 Jul 25. 16870440
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  26. Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT: 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. Bioorg Med Chem Lett. 2007 Apr 15;17(8):2210-5. Epub 2007 Feb 8. 17314045
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  29. Chegwidden WR, Wagner LE, Venta PJ, Bergenhem NC, Yu YS, Tashian RE: Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I. Hum Mutat. 1994;4(4):294-6. 7866410