炭酸脱水酵素I
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)』「2012/12/03 20:17:38」(JST)
[Wiki en表示]
Carbonic anhydrase I |
PDB rendering based on 1azm. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1AZM, 1BZM, 1CRM, 1CZM, 1HCB, 1HUG, 1HUH, 1J9W, 1JV0, 2CAB, 2FOY, 2FW4, 2IT4, 2NMX, 2NN1, 2NN7, 3LXE
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Identifiers |
Symbols |
CA1; CA-I; CAB; Car1 |
External IDs |
OMIM: 114800 MGI: 88268 HomoloGene: 20414 ChEMBL: 261 GeneCards: CA1 Gene |
EC number |
4.2.1.1 |
Gene Ontology |
Molecular function |
• carbonate dehydratase activity
• zinc ion binding
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Cellular component |
• cytoplasm
• Golgi apparatus
• cytosol
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Biological process |
• one-carbon metabolic process
• 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 |
759 |
12346 |
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Ensembl |
ENSG00000133742 |
ENSMUSG00000027556 |
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UniProt |
P00915 |
P13634 |
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RefSeq (mRNA) |
NM_001128829.2 |
NM_001083957.1 |
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RefSeq (protein) |
NP_001122301.1 |
NP_001077426.1 |
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Location (UCSC) |
Chr 8:
86.24 – 86.29 Mb |
Chr 3:
14.77 – 14.78 Mb |
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PubMed search |
[1] |
[2] |
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Carbonic anhydrase 1 is an enzyme that in humans is encoded by the CA1 gene.[1][2]
Carbonic 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.[2]
References
- ^ Lowe N, Edwards YH, Edwards M, Butterworth PH (Nov 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". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=759.
Further reading
- Tashian RE, Carter ND (1977). "Biochemical genetics of carbonic anhydrase.". Adv. Hum. Genet. 7: 1–56. PMID 827930.
- 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.
- Kendall AG, Tashian RE (1977). "Erythrocyte carbonic anhydrase I: inherited deficiency in humans.". Science 197 (4302): 471–2. doi:10.1126/science.406674. PMID 406674.
- Kannan KK, Notstrand B, Fridborg K, et al. (1975). "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. 72 (1): 51–5. doi:10.1073/pnas.72.1.51. PMC 432238. PMID 804171. //www.ncbi.nlm.nih.gov/pmc/articles/PMC432238/.
- 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.
- Lowe N, Brady HJ, Barlow JH, et al. (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 (1986). "Immunohistochemical observations on carbonic anhydrase I and II in human salivary glands and submandibular obstructive adenitis.". J. Oral Pathol. 15 (4): 187–90. doi:10.1111/j.1600-0714.1986.tb00604.x. PMID 3088232.
- Barlow JH, Lowe N, Edwards YH, Butterworth PH (1987). "Human carbonic anhydrase I cDNA.". Nucleic Acids Res. 15 (5): 2386. doi:10.1093/nar/15.5.2386. PMC 340641. PMID 3104879. //www.ncbi.nlm.nih.gov/pmc/articles/PMC340641/.
- Edwards YH, Barlow JH, Konialis CP, et al. (1988). "Assignment of the gene determining human carbonic anhydrase, CAI, to chromosome 8.". Ann. Hum. Genet. 50 (Pt 2): 123–9. doi:10.1111/j.1469-1809.1986.tb01030.x. PMID 3124707.
- Lin KT, Deutsch HF (1974). "Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.". J. Biol. Chem. 249 (8): 2329–37. 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 (1972). "Amino acid sequence of human erythrocyte carbonic anhydrase B.". Biochem. Biophys. Res. Commun. 48 (3): 670–7. doi:10.1016/0006-291X(72)90400-7. PMID 4625868.
- Lin KT, Deutsch HF (1973). "Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.". J. Biol. Chem. 248 (6): 1885–93. PMID 4632246.
- Omoto K, Ueda S, Goriki K, et al. (1981). "Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam.". Am. J. Hum. Genet. 33 (1): 105–11. PMC 1684865. PMID 6781336. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1684865/.
- Chegwidden WR, Wagner LE, Venta PJ, et al. (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.". Hum. Mutat. 4 (4): 294–6. doi:10.1002/humu.1380040411. PMID 7866410.
- Bekku S, Mochizuki H, Takayama E, et al. (1999). "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. PMID 9879596.
- Puscas I, Coltau M, Baican M, et al. (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.
PDB gallery
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1azm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1bzm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1crm: STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES
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1czm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1hcb: ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE
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1hug: DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES
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1huh: DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES
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1j9w: Solution Structure of the CAI Michigan 1 Variant
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1jv0: THE CRYSTAL STRUCTURE OF THE ZINC(II) ADDUCT OF THE CAI MICHIGAN 1 VARIANT
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2cab: STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
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2foy: Human Carbonic Anhydrase I complexed with a two-prong inhibitor
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2fw4: Carbonic anhydrase activators. The first X-ray crystallographic study of an activator of isoform I, structure with L-histidine.
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2nmx: Structure of inhibitor binding to Carbonic Anhydrase I
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2nn1: Structure of inhibitor binding to Carbonic Anhydrase I
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2nn7: Structure of inhibitor binding to Carbonic Anhydrase I
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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
- A proteomic study of protein variation between osteopenic and age-matched control bone tissue.
- Chaput CD, Dangott LJ, Rahm MD, Hitt KD, Stewart DS, Wayne Sampson H.SourceDepartment of Orthopedic Surgery, Scott & White Clinic.
- Experimental biology and medicine (Maywood, N.J.).Exp Biol Med (Maywood).2012 May 1;237(5):491-8. Epub 2012 May 22.
- The focus of this study was to identify changes in protein expression within the bone tissue environment between osteopenic and control bone tissue of human femoral neck patients with osteoarthritis. Femoral necks were compared from osteopenic patients and age-matched controls. A new method of bone
- PMID 22619369
- In vitro effects of some anabolic compounds on erythrocyte carbonic anhydrase I and II.
- Gençer N, Ergün A, Demir D.SourceChemistry Department/Biochemistry Div., Balikesir University, Cagis Kampus, Balikesir 10145, Turkey. ngencer@balikesir.edu.tr
- Journal of enzyme inhibition and medicinal chemistry.J Enzyme Inhib Med Chem.2012 Apr;27(2):208-10. Epub 2011 Jun 3.
- The in vitro effects of the anabolic compounds, zeranol, 17 β-estradiol, diethylstilbestrol (DES), and trenbolone, on the activity of purified human carbonic anhydrase I and II were evaluated. In vitro CA enzyme activity was determined colorimetrically using the CO₂ hydration method of Maren. IC�
- PMID 21635213
Japanese Journal
- 炭酸脱水酵素阻害薬 (特集 利尿薬およびそれに関連する話題)
- プロスタグランジン関連点眼液併用下でのβ遮断点眼液あるいは炭酸脱水酵素阻害点眼液から1%ドルソラミド塩酸塩・0.5%チモロールマレイン酸塩配合点眼液への変更時の眼圧下降効果と安全性
- CLINICAL INVESTIGATION : Persistence with topical glaucoma therapy among newly diagnosed Japanese patients
- Kashiwagi Kenji,Furuya Toshie
- Japanese journal of ophthalmology : the official international journal of the Japanese Ophthalmological Society 58(1), 68-74, 2014-01
- NAID 40019946937
Related Links
- "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 ...
- Carbonic Anhydrase in Health and Disease Since this enzyme produces and uses protons and bicarbonate ions, carbonic anhydrase plays a key role in the regulation of pH and fluid balance in different parts of our body. In our ...
★リンクテーブル★
[★]
[★]
- 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