炭酸脱水酵素III
WordNet
- an abundant nonmetallic tetravalent element occurring in three allotropic forms: amorphous carbon and graphite and diamond; occurs in all organic compounds (同)C, atomic number 6
- a copy made with carbon paper (同)carbon_copy
- the 9th letter of the Roman alphabet (同)i
PrepTutorEJDIC
- 『炭素』(化学記号は『C』) / 〈C〉炭素棒 / 〈C〉《時に〈U〉》=carbon paper
- 『私は』私が
- iodineの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/10/29 22:22:40」(JST)
[Wiki en表示]
Carbonic anhydrase III, muscle specific |
PDB rendering based on 1flj. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1Z93, 1Z97, 2HFW, 3UYN, 3UYQ
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Identifiers |
Symbols |
CA3; CAIII; Car3 |
External IDs |
OMIM: 114750 MGI: 88270 HomoloGene: 31298 ChEMBL: 2885 GeneCards: CA3 Gene |
EC number |
4.2.1.1 |
Gene Ontology |
Molecular function |
• carbonate dehydratase activity
• zinc ion binding
• nickel cation binding
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Cellular component |
• cytosol
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Biological process |
• one-carbon metabolic process
• response to oxidative stress
• bicarbonate transport
• small molecule metabolic process
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
761 |
12350 |
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Ensembl |
ENSG00000164879 |
ENSMUSG00000027559 |
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UniProt |
P07451 |
P16015 |
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RefSeq (mRNA) |
NM_005181.3 |
NM_007606.3 |
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RefSeq (protein) |
NP_005172.1 |
NP_031632.2 |
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Location (UCSC) |
Chr 8:
86.29 – 86.36 Mb |
Chr 3:
14.86 – 14.87 Mb |
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PubMed search |
[1] |
[2] |
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Carbonic anhydrase 3 is an enzyme that in humans is encoded by the CA3 gene.[1]
Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encode carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue-specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns.[2]
References
- ^ Shima K, Tashiro K, Hibi N, Tsukada Y, Hirai H (Jun 1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathol 59 (3): 237–9. doi:10.1007/BF00703210. PMID 6221502.
- ^ "Entrez Gene: CA3 carbonic anhydrase III, muscle specific". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=761.
Further reading
- Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies.". Annu. Rev. Biochem. 64: 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
- Carter N, Jeffery S, Shiels A, et al. (1980). "Characterization of human carbonic anhydrase III from skeletal muscle.". Biochem. Genet. 17 (9–10): 837–54. doi:10.1007/BF00504307. PMID 120192.
- Oikarinen A, Vuori J, Autio P, et al. (1993). "Comparison of muscle-derived serum carbonic anhydrase III and myoglobin in dermatological patients: effects of isotretinoin treatment". Acta Derm. Venereol. 72 (5): 352–4. PMID 1361281.
- Oguni M, Setogawa T, Tanaka O, et al. (1992). "Immunohistochemical study of carbonic anhydrase III in the extraocular muscles of human embryos". Acta Anat (Basel) 144 (4): 316–9. doi:10.1159/000147322. PMID 1414196.
- Vuori J, Rasi S, Takala T, Väänänen K (1992). "Dual-label time-resolved fluoroimmunoassay for simultaneous detection of myoglobin and carbonic anhydrase III in serum". Clin. Chem. 37 (12): 2087–92. PMID 1764784.
- Shamsutdinov NSh, Islamov RI, Valuillin VV (1991). "[Carbonic anhydrase III--a marker of the myoepithelial cells of human salivary glands]". Biulleten' eksperimental'noĭ biologii i meditsiny 111 (3): 320–1. PMID 1905166.
- Nork TM, Wallow IH, Sramek SJ, et al. (1990). "Immunocytochemical study of an eye with proliferative vitreoretinopathy and retinal tacks". Retina (Philadelphia, Pa.) 10 (1): 78–85. PMID 1971453.
- Lloyd J, Brownson C, Tweedie S, et al. (1987). "Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues". Genes Dev. 1 (6): 594–602. doi:10.1101/gad.1.6.594. PMID 2824285.
- Lloyd JC, Isenberg H, Hopkinson DA, Edwards YH (1986). "Isolation of a cDNA clone for the human muscle specific carbonic anhydrase, CAIII". Ann. Hum. Genet. 49 (Pt 3): 241–51. doi:10.1111/j.1469-1809.1985.tb01698.x. PMID 3000276.
- Lloyd J, McMillan S, Hopkinson D, Edwards YH (1986). "Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase". Gene 41 (2–3): 233–9. doi:10.1016/0378-1119(86)90103-4. PMID 3086182.
- Wade R, Gunning P, Eddy R, et al. (1987). "Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes". Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9571–5. doi:10.1073/pnas.83.24.9571. PMC 387182. PMID 3099285. //www.ncbi.nlm.nih.gov/pmc/articles/PMC387182/.
- Väänänen HK, Autio-Harmainen H (1987). "Carbonic anhydrase III: a new histochemical marker for myoepithelial cells". J. Histochem. Cytochem. 35 (6): 683–6. PMID 3106467.
- Nakagawa Y, Perentes E, Rubinstein LJ (1987). "Non-specificity of anti-carbonic anhydrase C antibody as a marker in human neurooncology". J. Neuropathol. Exp. Neurol. 46 (4): 451–60. doi:10.1097/00005072-198707000-00004. PMID 3110380.
- Edwards YH, Lloyd J, Parkar M, Povey S (1988). "The gene for human muscle specific carbonic anhydrase (CAIII) is assigned to chromosome 8". Ann. Hum. Genet. 50 (Pt 1): 41–7. doi:10.1111/j.1469-1809.1986.tb01937.x. PMID 3122635.
- Väänänen HK, Paloniemi M, Vuori J (1985). "Purification and localization of human carbonic anhydrase. III. Typing of skeletal muscle fibers in paraffin embedded sections". Histochemistry 83 (3): 231–5. PMID 3930440.
- Carter ND, Heath R, Jeffery S, Rodeck C (1982). "Fetal plasma carbonic anhydrase III in Duchenne dystrophy". Lancet 1 (8262): 39–40. doi:10.1016/S0140-6736(82)92574-0. PMID 6119426.
- Heath R, Schwartz MS, Brown IR, Carter ND (1983). "Carbonic anhydrase III in neuromuscular disorders". J. Neurol. Sci. 59 (3): 383–8. doi:10.1016/0022-510X(83)90023-0. PMID 6410007.
- Wåhlstrand T, Wistrand PJ (1980). "Carbonic anhydrase C in the human renal medulla". Ups. J. Med. Sci. 85 (1): 7–17. doi:10.3109/03009738009179167. PMID 6770531.
- Jeffery S, Edwards Y, Carter N (1981). "Distribution of CAIII in fetal and adult human tissue". Biochem. Genet. 18 (9–10): 843–9. doi:10.1007/BF00500117. PMID 6784712.
PDB gallery
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1flj: CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III
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1z93: Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.
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1z97: Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.
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2hfw: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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2hfx: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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2hfy: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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Carbonic anhydrases
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- CA1
- CA2
- CA3
- CA4
- CA5A
- CA5B
- CA6
- CA7
- CA8
- CA9
- CA10
- CA11
- CA12
- CA13
- CA14
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UpToDate Contents
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English Journal
- Novel application of acetazolamide to reduce cerebrospinal fluid production in patients undergoing thoracoabdominal aortic surgery.
- Jafarzadeh F, Field ML, Harrington DK, Kuduvalli M, Oo A, Kendall J, Desmond M, Mills K.Author information Institute of Cardiovascular Medicine and Science, Thoracic Aortic Aneurysm Service, Liverpool Heart and Chest Hospital, Liverpool, UK.AbstractOBJECTIVES: Paraplegia is a rare but devastating complication, which may follow thoracoabdominal aortic surgery. Many adjuncts have been developed to reduce this risk including cerebrospinal fluid (CSF) drainage. Acetazolamide (carbonic anhydrase inhibitor) is a drug used to counteract mountain sickness and one of its effects is to reduce CSF production. Here, we report its first postoperative application in thoracoabdominal surgery with the aim of reducing cerebrospinal cord perfusion pressure and reducing risk of paraplegia.
- Interactive cardiovascular and thoracic surgery.Interact Cardiovasc Thorac Surg.2014 Jan;18(1):21-6. doi: 10.1093/icvts/ivt384. Epub 2013 Oct 14.
- OBJECTIVES: Paraplegia is a rare but devastating complication, which may follow thoracoabdominal aortic surgery. Many adjuncts have been developed to reduce this risk including cerebrospinal fluid (CSF) drainage. Acetazolamide (carbonic anhydrase inhibitor) is a drug used to counteract mountain sick
- PMID 24130087
- Proteomic identification of gravitropic response genes in peanut gynophores.
- Li HF, Zhu FH, Li HY, Zhu W, Chen XP, Hong YB, Liu HY, Wu H, Liang XQ.Author information Crops Research Institute, Guangdong Academy of Agricultural Sciences, Wushan 510640, Guangzhou, China. Electronic address: 565340390@163.com.AbstractPeanut (Arachis hypogaea L.) is one of the most important oil-bearing crops in the world. The gravitropic response of peanut gynophores plays an essential role in peanut reproductive development. In this study, we developed an in vitro culture system and applied it to the study of peanut gynophore gravitropism. By comparing the proteomes of gynophores grown in vitro with the tip pointing upward (gravity stimulation sample) and downward (natural growth control) at 6h and 12h, we observed 42 and 39 with significantly altered expression pattern at 6 and 12h, respectively. Out of these proteins, 13 proteins showed same expression profiling at both 6h and 12h. They were identified by MALDI-TOF/TOF and further characterized with quantitative real time RT-PCR. Among the 13 identified proteins, two were identified as class III acidic endochitinases, two were identified as Kunitz trypsin protease inhibitors, and the remaining proteins were identified as pathogenesis-related class 10 protein, Ara h 8 allergen isoform 3, voltage-dependent anion channel, gamma carbonic anhydrase 1, germin-like protein subfamily 3 member 3 precursor, chloride channel, glycine-rich RNA-binding protein and gibberellin receptor GID1. Real time RT-PCR analysis revealed that transcriptional regulation is consistent with expression at the protein level for class III acidic endochitinase, Kunitz trypsin protease inhibitor, chloride channel and pathogenesis-related class 10 protein, while the expression of the other 7 proteins might be regulated at post-transcriptional levels. This study identified several potential gravitropic response proteins in peanut gynophores and helps to understand early gravitropic responses in peanut gynophores.
- Journal of proteomics.J Proteomics.2013 Nov 20;93:303-13. doi: 10.1016/j.jprot.2013.08.006. Epub 2013 Aug 28.
- Peanut (Arachis hypogaea L.) is one of the most important oil-bearing crops in the world. The gravitropic response of peanut gynophores plays an essential role in peanut reproductive development. In this study, we developed an in vitro culture system and applied it to the study of peanut gynophore g
- PMID 23994445
- Inhibition of human carbonic anhydrase isoforms I-XIV with sulfonamides incorporating fluorine and 1,3,5-triazine moieties.
- Ceruso M, Vullo D, Scozzafava A, Supuran CT.Author information Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.AbstractReaction of cyanuryl fluoride with sulfanilamide or 4-aminoethylbenzenesulfonamide afforded triazinyl-substituted benzenesulfonamides incorporating fluorine, which were further derivatized by reaction with amines, amino alcohols, amino acids or amino acid esters. Inhibition studies of all the human (h) carbonic anhydrase (CA, EC 4.2.1.1) isoforms, hCA I-XIV with these compounds revealed that they show moderate-weak inhibition of hCA III, IV, VA and XIII, rather moderate inhibition against hCA I, VI, and IX, and excellent inhibition of the physiologically relevant hCA II, VII and XII. The inhibition profile of these fluorine containing triazinyl sulfonamides is thus very different from the corresponding analogs incorporating chlorine, which were previously investigated as inhibitors of some of these enzymes.
- Bioorganic & medicinal chemistry.Bioorg Med Chem.2013 Nov 15;21(22):6929-36. doi: 10.1016/j.bmc.2013.09.031. Epub 2013 Sep 19.
- Reaction of cyanuryl fluoride with sulfanilamide or 4-aminoethylbenzenesulfonamide afforded triazinyl-substituted benzenesulfonamides incorporating fluorine, which were further derivatized by reaction with amines, amino alcohols, amino acids or amino acid esters. Inhibition studies of all the human
- PMID 24103430
Japanese Journal
- Early changes in proteome levels upon acute deltamethrin exposure in mammalian skin system associated with its neoplastic transformation potential
- Bacillus thuringiensis Cry Toxins Bound Specifically to Various Proteins via Domain III, Which Had a Galactose-Binding Domain-Like Fold
- Bioscience, biotechnology, and biochemistry 75(2), 305-312, 2011-02-23
- NAID 10027897803
Related Links
- P, Eddy R, Shows T, Kedes L: Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely ...
- Introduction Carbonic anhydrase III (CAIII) belongs to a family of structurally related enzymes that catalyze the reversible hydration of carbon dioxide (H 2 O + CO 2 ↔ HCO 3 - + H+) [1, 2]. The CA isoenzymes are involved in ...
★リンクテーブル★
[★]
- 英
- carbonic anhydrase III
[★]
[★]
[★]
- 関
- C、carbon、carbonate、carbonic acid
[★]
アンヒドラーゼ、脱水酵素
- 関
- dehydrase、dehydratase
[★]
炭素、カーボン
- 関
- C、carbonic