They show extensive diversity in tissue distribution and in their subcellular localization. CA1 is closely linked to CA2 and CA3 genes on chromosome 8, and it encodes a cytosolic protein which is found at the highest level in erythrocytes. Transcript variants of CA1 utilizing alternative polyA_sites have been described in literature.[6]
The human CA1 protein contains an N-terminus active site, zinc binding site, and substrate-binding site.[7] The crystal structure of the human CA1-bicarbonate anion complex reveals the geometry of two H-bonds between the Glu106-Thr199 pair and the Glu117-His119 pair, and one pi H-bond between a water molecule and the phenyl ring of the Tyr114 residue. The product inhibition of CA1 via bicarbonate anions is correlated to the proton localization change on His119. So the Glu117-His119 H-bond is considered to regulate the ionicity of the zinc ion and the binding strength of the bicarbonate anion.[8]
Mechanismedit
The reaction catalyzed by CA1 is the same as other carbonic anhydrase family proteins:
The CA1-catalyzed reaction has a relatively low reaction affinity (Km) of 4.0 mM for CO2,[7][10]turnover number (Kcat) of 2×105 s−1, and catalytic efficiency (Kcat/Km) of 5×107 M−1s−1 comparing to other isozymes of the α-CA family of carbonic anhydrases. The turnover rate and catalytic rate of CA1 are only about 10% that of CA2 (Kcat: 1.4×106 s−1, Kcat/Km: 1.5×108 M−1s−1).[11]
Functionedit
Carbonic anhydrase 1 belongs to α-CA sub-family and is localized in the cytosol of red blood cell, GI tract, cardiac tissues and other organs or tissues.[12] Transmembrane transport of CA-produced bicarbonate contributes significantly to cellular pH regulation.[13]
In a human zinc-activated variant of CA1, the Michigan Variant, a single point mutation changes His 67 to Arg in a critical region of the active site. This variant of the zinc metalloenzyme appears to be unique in that it possesses esterase activity that is specifically enhanced by added free zinc ions.[14]
As CA1 is an important therapeutic target, development of its inhibitors will contribute to disease treatment. Compared to other CA family members, CA1 has relatively low affinity to common CA inhibitors.[16] Nonetheless, it has medium affinity for CA inhibitor sulfonamides.[citation needed]
^ abcGRCh38: Ensembl release 89: ENSG00000133742 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000027556 - 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.
^Lowe N, Edwards YH, Edwards M, Butterworth PH (Aug 1991). "Physical mapping of the human carbonic anhydrase gene cluster on chromosome 8". Genomics. 10 (4): 882–8. doi:10.1016/0888-7543(91)90176-F. PMID 1916821.
^Kumar V, Kannan KK (Aug 1994). "Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate". Journal of Molecular Biology. 241 (2): 226–32. doi:10.1006/jmbi.1994.1491. PMID 8057362.
^Carbonic acid has a pKa of around 6.36 (the exact value depends on the medium) so at pH 7 a small percentage of the bicarbonate is protonated. See carbonic acid for details concerning the equilibria HCO− 3 + H+ ⇌ H2CO3 and H2CO3 ⇌ CO2 + H2O
^Briganti F, Mangani S, Scozzafava A, Vernaglione G, Supuran CT (Oct 1999). "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?". Journal of Biological Inorganic Chemistry. 4 (5): 528–36. doi:10.1007/s007750050375. PMID 10550681. S2CID 25890428.
^Silverman DN, Lindskog S (2002-05-01). "The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water". Accounts of Chemical Research. 21 (1): 30–36. doi:10.1021/ar00145a005.
^ abcTorella D, Ellison GM, Torella M, Vicinanza C, Aquila I, Iaconetti C, Scalise M, Marino F, Henning BJ, Lewis FC, Gareri C, Lascar N, Cuda G, Salvatore T, Nappi G, Indolfi C, Torella R, Cozzolino D, Sasso FC (2014-01-01). "Carbonic anhydrase activation is associated with worsened pathological remodeling in human ischemic diabetic cardiomyopathy". Journal of the American Heart Association. 3 (2): e000434. doi:10.1161/JAHA.113.000434. PMC4187518. PMID 24670789.
^Alvarez BV, Quon AL, Mullen J, Casey JR (2013-01-01). "Quantification of carbonic anhydrase gene expression in ventricle of hypertrophic and failing human heart". BMC Cardiovascular Disorders. 13: 2. doi:10.1186/1471-2261-13-2. PMC3570296. PMID 23297731.
^Ferraroni M, Tilli S, Briganti F, Chegwidden WR, Supuran CT, Wiebauer KE, Tashian RE, Scozzafava A (May 2002). "Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination". Biochemistry. 41 (20): 6237–44. doi:10.1021/bi0120446. PMID 12009884.
^Gao BB, Clermont A, Rook S, Fonda SJ, Srinivasan VJ, Wojtkowski M, Fujimoto JG, Avery RL, Arrigg PG, Bursell SE, Aiello LP, Feener EP (Feb 2007). "Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation". Nature Medicine. 13 (2): 181–8. doi:10.1038/nm1534. PMID 17259996. S2CID 14404913.
^Supuran CT (Feb 2008). "Carbonic anhydrases: novel therapeutic applications for inhibitors and activators". Nature Reviews. Drug Discovery. 7 (2): 168–81. doi:10.1038/nrd2467. PMID 18167490. S2CID 3833178.
^Rolland T, Taşan M, Charloteaux B, Pevzner SJ, Zhong Q, Sahni N, et al. (Nov 2014). "A proteome-scale map of the human interactome network". Cell. 159 (5): 1212–26. doi:10.1016/j.cell.2014.10.050. PMC4266588. PMID 25416956.
^Wang J, Huo K, Ma L, Tang L, Li D, Huang X, et al. (2011-01-01). "Toward an understanding of the protein interaction network of the human liver". Molecular Systems Biology. 7: 536. doi:10.1038/msb.2011.67. PMC3261708. PMID 21988832.
^Vinayagam A, Stelzl U, Foulle R, Plassmann S, Zenkner M, Timm J, Assmus HE, Andrade-Navarro MA, Wanker EE (Sep 2011). "A directed protein interaction network for investigating intracellular signal transduction". Science Signaling. 4 (189): rs8. doi:10.1126/scisignal.2001699. PMID 21900206. S2CID 7418133.
External linksedit
Human CA1 genome location and CA1 gene details page in the UCSC Genome Browser.
Further readingedit
Tashian RE, Carter ND (1976). "Biochemical Genetics of Carbonic Anhydrase". Advances in Human Genetics. Vol. 7. pp. 1–56. doi:10.1007/978-1-4757-0659-8_1. ISBN978-1-4757-0661-1. PMID 827930.
Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annual Review of Biochemistry. 64 (1): 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
Kannan KK, Notstrand B, Fridborg K, Lövgren S, Ohlsson A, Petef M (Jan 1975). "Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution" (PDF). Proceedings of the National Academy of Sciences of the United States of America. 72 (1): 51–5. doi:10.1073/pnas.72.1.51. PMC432238. PMID 804171.
Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Lowe N, Brady HJ, Barlow JH, Sowden JC, Edwards M, Butterworth PH (Sep 1990). "Structure and methylation patterns of the gene encoding human carbonic anhydrase I". Gene. 93 (2): 277–83. doi:10.1016/0378-1119(90)90236-K. PMID 2121614.
Noda Y, Sumitomo S, Hikosaka N, Mori M (Apr 1986). "Immunohistochemical observations on carbonic anhydrase I and II in human salivary glands and submandibular obstructive adenitis". Journal of Oral Pathology. 15 (4): 187–90. doi:10.1111/j.1600-0714.1986.tb00604.x. PMID 3088232.
Edwards YH, Barlow JH, Konialis CP, Povey S, Butterworth PH (May 1986). "Assignment of the gene determining human carbonic anhydrase, CAI, to chromosome 8". Annals of Human Genetics. 50 (Pt 2): 123–9. doi:10.1111/j.1469-1809.1986.tb01030.x. PMID 3124707. S2CID 44919686.
Lin KT, Deutsch HF (Apr 1974). "Human carbonic anhydrases. XII. The complete primary structure of the C isozyme". The Journal of Biological Chemistry. 249 (8): 2329–37. doi:10.1016/S0021-9258(19)42734-8. PMID 4207120.
Giraud N, Marriq C, Laurent-Tabusse G (1975). "[Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)]". Biochimie. 56 (8): 1031–43. doi:10.1016/S0300-9084(74)80093-3. PMID 4217196.
Andersson B, Nyman PO, Strid L (Aug 1972). "Amino acid sequence of human erythrocyte carbonic anhydrase B". Biochemical and Biophysical Research Communications. 48 (3): 670–7. doi:10.1016/0006-291X(72)90400-7. PMID 4625868.
Lin KT, Deutsch HF (Mar 1973). "Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B". The Journal of Biological Chemistry. 248 (6): 1885–93. doi:10.1016/S0021-9258(19)44161-6. PMID 4632246.
Omoto K, Ueda S, Goriki K, Takahashi N, Misawa S, Pagaran IG (Jan 1981). "Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam". American Journal of Human Genetics. 33 (1): 105–11. PMC1684865. PMID 6781336.
Chegwidden WR, Wagner LE, Venta PJ, Bergenhem NC, Yu YS, Tashian RE (1995). "Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I". Human Mutation. 4 (4): 294–6. doi:10.1002/humu.1380040411. PMID 7866410. S2CID 21458184.
Bekku S, Mochizuki H, Takayama E, Shinomiya N, Fukamachi H, Ichinose M, Tadakuma T, Yamamoto T (Dec 1998). "Carbonic anhydrase I and II as a differentiation marker of human and rat colonic enterocytes". Research in Experimental Medicine. Zeitschrift für die Gesamte Experimentelle Medizin Einschliesslich Experimenteller Chirurgie. 198 (4): 175–85. doi:10.1007/s004330050101. PMID 9879596. S2CID 11297322.
Puscas I, Coltau M, Baican M, Pasca R, Domuta G, Hecht A (2001). "Vasoconstrictive drugs increase carbonic anhydrase I in vascular smooth muscle while vasodilating drugs reduce the activity of this isozyme by a direct mechanism of action". Drugs Under Experimental and Clinical Research. 27 (2): 53–60. PMID 11392054.
April 11, 2024
gene, carbonic, anhydrase, enzyme, that, humans, encoded, gene, ca1available, structurespdbortholog, search, pdbe, rcsblist, codes1azm, 1bzm, 1crm, 1czm, 1hcb, 1hug, 1huh, 1j9w, 1jv0, 2cab, 2foy, 2fw4, 2it4, 2nmx, 2nn1, 2nn7, 3lxe, 3w6h, 3w6i, 4wr7, 4wup, 4wuq. Carbonic anhydrase 1 is an enzyme that in humans is encoded by the CA1 gene 5 6 CA1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1AZM 1BZM 1CRM 1CZM 1HCB 1HUG 1HUH 1J9W 1JV0 2CAB 2FOY 2FW4 2IT4 2NMX 2NN1 2NN7 3LXE 3W6H 3W6I 4WR7 4WUP 4WUQIdentifiersAliasesCA1 CA I CAB Car1 HEL S 11 carbonic anhydrase 1External IDsOMIM 114800 MGI 88268 HomoloGene 20414 GeneCards CA1Gene location Human Chr Chromosome 8 human 1 Band8q21 2Start85 327 608 bp 1 End85 379 014 bp 1 Gene location Mouse Chr Chromosome 3 mouse 2 Band3 A1 3 3 18 cMStart14 831 276 bp 2 End14 873 428 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inspongy bonerectumbone marrow cellsmonocytebloodsuperficial temporal arteryspleenright lungamniotic fluidgerminal epitheliumTop expressed inleft colonspleenfemurbody of femurbone marrowleft lobe of livercervixpretectal areabloodcochleaMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmetal ion binding zinc ion binding lyase activity hydro lyase activity arylesterase activity protein binding carbonate dehydratase activity carbonic anhydraseCellular componentextracellular exosome cytosol cytoplasmBiological processone carbon metabolic process bicarbonate transport interleukin 12 mediated signaling pathwaySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez75912346EnsemblENSG00000133742ENSMUSG00000027556UniProtP00915P13634RefSeq mRNA NM 001128829NM 001128830NM 001128831NM 001164830NM 001291967NM 001291968NM 001738NM 001083957NM 009799RefSeq protein NP 001122301NP 001122302NP 001122303NP 001158302NP 001278896NP 001278897NP 001729NP 001077426NP 033929Location UCSC Chr 8 85 33 85 38 MbChr 3 14 83 14 87 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseCarbonic anhydrases CAs are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide They participate in a variety of biological processes including cellular respiration calcification acid base balance bone resorption and the formation of aqueous humor cerebrospinal fluid saliva and gastric acid They show extensive diversity in tissue distribution and in their subcellular localization CA1 is closely linked to CA2 and CA3 genes on chromosome 8 and it encodes a cytosolic protein which is found at the highest level in erythrocytes Transcript variants of CA1 utilizing alternative polyA sites have been described in literature 6 Contents 1 Structure 2 Mechanism 3 Function 4 Clinical significance 5 Interactions 6 References 7 External links 8 Further readingStructure editThe human CA1 protein contains an N terminus active site zinc binding site and substrate binding site 7 The crystal structure of the human CA1 bicarbonate anion complex reveals the geometry of two H bonds between the Glu106 Thr199 pair and the Glu117 His119 pair and one pi H bond between a water molecule and the phenyl ring of the Tyr114 residue The product inhibition of CA1 via bicarbonate anions is correlated to the proton localization change on His119 So the Glu117 His119 H bond is considered to regulate the ionicity of the zinc ion and the binding strength of the bicarbonate anion 8 Mechanism editThe reaction catalyzed by CA1 is the same as other carbonic anhydrase family proteins CO2 H2O Carbonic anhydraseH2CO3 displaystyle ce CO2 H2O gt atop ce Carbonic anhydrase H2CO3 nbsp in tissues high CO2 concentration 9 The CA1 catalyzed reaction has a relatively low reaction affinity Km of 4 0 mM for CO2 7 10 turnover number Kcat of 2 105 s 1 and catalytic efficiency Kcat Km of 5 107 M 1s 1 comparing to other isozymes of the a CA family of carbonic anhydrases The turnover rate and catalytic rate of CA1 are only about 10 that of CA2 Kcat 1 4 106 s 1 Kcat Km 1 5 108 M 1s 1 11 Function editCarbonic anhydrase 1 belongs to a CA sub family and is localized in the cytosol of red blood cell GI tract cardiac tissues and other organs or tissues 12 Transmembrane transport of CA produced bicarbonate contributes significantly to cellular pH regulation 13 In a human zinc activated variant of CA1 the Michigan Variant a single point mutation changes His 67 to Arg in a critical region of the active site This variant of the zinc metalloenzyme appears to be unique in that it possesses esterase activity that is specifically enhanced by added free zinc ions 14 Clinical significance editCA1 activation is associated with worsened pathological remodeling in human ischemic diabetic cardiomyopathy 12 In diabetic mellitus type 2 patients with postinfarct heart failure who were undergoing surgical coronary revascularization myocardial levels of CA1 were sixfold higher than nondiabetic patients Elevated CA1 expression was mainly localized in the cardiac interstitium and endothelial cells Furthermore high glucose induced elevation of CA1 hampers endothelial cell permeability and determines endothelial cell apoptosis in vitro 12 CA1 also mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation and serine protease factor XIIa generation These phenomena induce proliferative diabetic retinopathy and diabetic macular edema disease progression which represent leading causes of vision loss 15 As CA1 is an important therapeutic target development of its inhibitors will contribute to disease treatment Compared to other CA family members CA1 has relatively low affinity to common CA inhibitors 16 Nonetheless it has medium affinity for CA inhibitor sulfonamides citation needed Interactions editCA1 has been shown to interact with TFCP2 17 HSD17B7 18 MAPK6 19 These interactions have been confirmed using the high throughput method one hit References edit a b c GRCh38 Ensembl release 89 ENSG00000133742 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000027556 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 Lowe N Edwards YH Edwards M Butterworth PH Aug 1991 Physical mapping of the human carbonic anhydrase gene cluster on chromosome 8 Genomics 10 4 882 8 doi 10 1016 0888 7543 91 90176 F PMID 1916821 a b Entrez Gene CA1 carbonic anhydrase I a b CA1 Carbonic anhydrase 1 Homo sapiens Human CA1 gene amp protein www uniprot org Retrieved 2016 03 23 Kumar V Kannan KK Aug 1994 Enzyme substrate interactions Structure of human carbonic anhydrase I complexed with bicarbonate Journal of Molecular Biology 241 2 226 32 doi 10 1006 jmbi 1994 1491 PMID 8057362 Carbonic acid has a pKa of around 6 36 the exact value depends on the medium so at pH 7 a small percentage of the bicarbonate is protonated See carbonic acid for details concerning the equilibria HCO 3 H H2CO3 and H2CO3 CO2 H2O Briganti F Mangani S Scozzafava A Vernaglione G Supuran CT Oct 1999 Carbonic anhydrase catalyzes cyanamide hydration to urea is it mimicking the physiological reaction Journal of Biological Inorganic Chemistry 4 5 528 36 doi 10 1007 s007750050375 PMID 10550681 S2CID 25890428 Silverman DN Lindskog S 2002 05 01 The catalytic mechanism of carbonic anhydrase implications of a rate limiting protolysis of water Accounts of Chemical Research 21 1 30 36 doi 10 1021 ar00145a005 a b c Torella D Ellison GM Torella M Vicinanza C Aquila I Iaconetti C Scalise M Marino F Henning BJ Lewis FC Gareri C Lascar N Cuda G Salvatore T Nappi G Indolfi C Torella R Cozzolino D Sasso FC 2014 01 01 Carbonic anhydrase activation is associated with worsened pathological remodeling in human ischemic diabetic cardiomyopathy Journal of the American Heart Association 3 2 e000434 doi 10 1161 JAHA 113 000434 PMC 4187518 PMID 24670789 Alvarez BV Quon AL Mullen J Casey JR 2013 01 01 Quantification of carbonic anhydrase gene expression in ventricle of hypertrophic and failing human heart BMC Cardiovascular Disorders 13 2 doi 10 1186 1471 2261 13 2 PMC 3570296 PMID 23297731 Ferraroni M Tilli S Briganti F Chegwidden WR Supuran CT Wiebauer KE Tashian RE Scozzafava A May 2002 Crystal structure of a zinc activated variant of human carbonic anhydrase I CA I Michigan 1 evidence for a second zinc binding site involving arginine coordination Biochemistry 41 20 6237 44 doi 10 1021 bi0120446 PMID 12009884 Gao BB Clermont A Rook S Fonda SJ Srinivasan VJ Wojtkowski M Fujimoto JG Avery RL Arrigg PG Bursell SE Aiello LP Feener EP Feb 2007 Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation Nature Medicine 13 2 181 8 doi 10 1038 nm1534 PMID 17259996 S2CID 14404913 Supuran CT Feb 2008 Carbonic anhydrases novel therapeutic applications for inhibitors and activators Nature Reviews Drug Discovery 7 2 168 81 doi 10 1038 nrd2467 PMID 18167490 S2CID 3833178 Rolland T Tasan M Charloteaux B Pevzner SJ Zhong Q Sahni N et al Nov 2014 A proteome scale map of the human interactome network Cell 159 5 1212 26 doi 10 1016 j cell 2014 10 050 PMC 4266588 PMID 25416956 Wang J Huo K Ma L Tang L Li D Huang X et al 2011 01 01 Toward an understanding of the protein interaction network of the human liver Molecular Systems Biology 7 536 doi 10 1038 msb 2011 67 PMC 3261708 PMID 21988832 Vinayagam A Stelzl U Foulle R Plassmann S Zenkner M Timm J Assmus HE Andrade Navarro MA Wanker EE Sep 2011 A directed protein interaction network for investigating intracellular signal transduction Science Signaling 4 189 rs8 doi 10 1126 scisignal 2001699 PMID 21900206 S2CID 7418133 External links editHuman CA1 genome location and CA1 gene details page in the UCSC Genome Browser Further reading editTashian RE Carter ND 1976 Biochemical Genetics of Carbonic Anhydrase Advances in Human Genetics Vol 7 pp 1 56 doi 10 1007 978 1 4757 0659 8 1 ISBN 978 1 4757 0661 1 PMID 827930 Sly WS Hu PY 1995 Human carbonic anhydrases and carbonic anhydrase deficiencies Annual Review of Biochemistry 64 1 375 401 doi 10 1146 annurev bi 64 070195 002111 PMID 7574487 Kendall AG Tashian RE Jul 1977 Erythrocyte carbonic anhydrase I inherited deficiency in humans Science 197 4302 471 2 Bibcode 1977Sci 197 471K doi 10 1126 science 406674 PMID 406674 Kannan KK Notstrand B Fridborg K Lovgren S Ohlsson A Petef M Jan 1975 Crystal structure of human erythrocyte carbonic anhydrase B Three dimensional structure at a nominal 2 2 A resolution PDF Proceedings of the National Academy of Sciences of the United States of America 72 1 51 5 doi 10 1073 pnas 72 1 51 PMC 432238 PMID 804171 Dawson SJ White LA May 1992 Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin The Journal of Infection 24 3 317 20 doi 10 1016 S0163 4453 05 80037 4 PMID 1602151 Lowe N Brady HJ Barlow JH Sowden JC Edwards M Butterworth PH Sep 1990 Structure and methylation patterns of the gene encoding human carbonic anhydrase I Gene 93 2 277 83 doi 10 1016 0378 1119 90 90236 K PMID 2121614 Noda Y Sumitomo S Hikosaka N Mori M Apr 1986 Immunohistochemical observations on carbonic anhydrase I and II in human salivary glands and submandibular obstructive adenitis Journal of Oral Pathology 15 4 187 90 doi 10 1111 j 1600 0714 1986 tb00604 x PMID 3088232 Barlow JH Lowe N Edwards YH Butterworth PH Mar 1987 Human carbonic anhydrase I cDNA Nucleic Acids Research 15 5 2386 doi 10 1093 nar 15 5 2386 PMC 340641 PMID 3104879 Edwards YH Barlow JH Konialis CP Povey S Butterworth PH May 1986 Assignment of the gene determining human carbonic anhydrase CAI to chromosome 8 Annals of Human Genetics 50 Pt 2 123 9 doi 10 1111 j 1469 1809 1986 tb01030 x PMID 3124707 S2CID 44919686 Lin KT Deutsch HF Apr 1974 Human carbonic anhydrases XII The complete primary structure of the C isozyme The Journal of Biological Chemistry 249 8 2329 37 doi 10 1016 S0021 9258 19 42734 8 PMID 4207120 Giraud N Marriq C Laurent Tabusse G 1975 Primary structure of human B erythrocyte carbonic anhydrase 3 Sequence of CNBr fragment I and III residues 149 260 Biochimie 56 8 1031 43 doi 10 1016 S0300 9084 74 80093 3 PMID 4217196 Andersson B Nyman PO Strid L Aug 1972 Amino acid sequence of human erythrocyte carbonic anhydrase B Biochemical and Biophysical Research Communications 48 3 670 7 doi 10 1016 0006 291X 72 90400 7 PMID 4625868 Lin KT Deutsch HF Mar 1973 Human carbonic anhydrases XI The complete primary structure of carbonic anhydrase B The Journal of Biological Chemistry 248 6 1885 93 doi 10 1016 S0021 9258 19 44161 6 PMID 4632246 Omoto K Ueda S Goriki K Takahashi N Misawa S Pagaran IG Jan 1981 Population genetic studies of the Philippine Negritos III Identification of the carbonic anhydrase 1 variant with CA1 Guam American Journal of Human Genetics 33 1 105 11 PMC 1684865 PMID 6781336 Chegwidden WR Wagner LE Venta PJ Bergenhem NC Yu YS Tashian RE 1995 Marked zinc activation of ester hydrolysis by a mutation 67 His CAT to Arg CGT in the active site of human carbonic anhydrase I Human Mutation 4 4 294 6 doi 10 1002 humu 1380040411 PMID 7866410 S2CID 21458184 Bekku S Mochizuki H Takayama E Shinomiya N Fukamachi H Ichinose M Tadakuma T Yamamoto T Dec 1998 Carbonic anhydrase I and II as a differentiation marker of human and rat colonic enterocytes Research in Experimental Medicine Zeitschrift fur die Gesamte Experimentelle Medizin Einschliesslich Experimenteller Chirurgie 198 4 175 85 doi 10 1007 s004330050101 PMID 9879596 S2CID 11297322 Puscas I Coltau M Baican M Pasca R Domuta G Hecht A 2001 Vasoconstrictive drugs increase carbonic anhydrase I in vascular smooth muscle while vasodilating drugs reduce the activity of this isozyme by a direct mechanism of action Drugs Under Experimental and Clinical Research 27 2 53 60 PMID 11392054 Retrieved from https en wikipedia org w index php title CA1 gene amp oldid 1173346900, wikipedia, wiki, book, books, library,
