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KEGG pathways | MAP code | Pathways |
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MAP00910 | Nitrogen metabolism |
UniProtKB:Accession Number | P17067 | P61517 |
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Entry name | CAHC_PEA | CAN_ECOLI |
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Activity | H(2)CO(3) = CO(2) + H(2)O. | H(2)CO(3) = CO(2) + H(2)O. |
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Subunit | Homohexamer. | Homodimer. |
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Subcellular location | Plastid, chloroplast stroma. |
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Cofactor |
| Binds 1 zinc ion per subunit. |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | Fig.4, p.1414-1415 | 4 | [5] | FIG.4, p.5526 | 4 | [6] | p.10305 |
| [7] | p.48615, p.48617 |
| [8] | p.919-920 |
| [9] | Fig.7, p.208 | 5 | [10] |
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| [11] |
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references | [1] |
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PubMed ID | 7925414 |
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Journal | Eur J Biochem |
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Year | 1994 |
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Volume | 224 |
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Pages | 901-7 |
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Authors | Johansson IM, Forsman C |
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Title | Solvent hydrogen isotope effects and anion inhibition of CO2 hydration catalysed by carbonic anhydrase from Pisum sativum. |
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[2] |
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PubMed ID | 9100024 |
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Journal | Biochemistry |
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Year | 1997 |
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Volume | 36 |
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Pages | 4287-94 |
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Authors | Bjorkbacka H, Johansson IM, Skarfstad E, Forsman C |
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Title | The sulfhydryl groups of Cys 269 and Cys 272 are critical for the oligomeric state of chloroplast carbonic anhydrase from Pisum sativum. |
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[3] |
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PubMed ID | 9336012 |
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Journal | Pharmacol Ther |
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Year | 1997 |
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Volume | 74 |
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Pages | 1-20 |
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Authors | Lindskog S |
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Title | Structure and mechanism of carbonic anhydrase. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 108-328. |
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Medline ID | 20211383 |
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PubMed ID | 10747009 |
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Journal | EMBO J |
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Year | 2000 |
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Volume | 19 |
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Pages | 1407-18 |
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Authors | Kimber MS, Pai EF |
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Title | The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases. |
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Related PDB | 1ekj |
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Related UniProtKB | P17067 |
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[5] |
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Comments | X-ray crystallography |
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PubMed ID | 10681531 |
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Journal | J Biol Chem |
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Year | 2000 |
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Volume | 275 |
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Pages | 5521-6 |
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Authors | Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T |
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Title | X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration. |
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Related PDB | 1ddz |
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[6] |
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Comments | X-ray crystallography |
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PubMed ID | 11096105 |
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Journal | J Biol Chem |
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Year | 2001 |
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Volume | 276 |
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Pages | 10299-305 |
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Authors | Strop P, Smith KS, Iverson TM, Ferry JG, Rees DC |
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Title | Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. |
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Related PDB | 1g5c |
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[7] |
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PubMed ID | 11696553 |
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Journal | J Biol Chem |
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Year | 2001 |
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Volume | 276 |
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Pages | 48615-8 |
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Authors | Tripp BC, Smith K, Ferry JG |
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Title | Carbonic anhydrase: new insights for an ancient enzyme. |
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[8] |
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PubMed ID | 11316870 |
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Journal | Protein Sci |
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Year | 2001 |
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Volume | 10 |
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Pages | 911-22 |
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Authors | Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY |
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Title | Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity. |
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Related PDB | 1i6o,1i6p |
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[9] |
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PubMed ID | 12147257 |
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Journal | Arch Biochem Biophys |
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Year | 2002 |
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Volume | 404 |
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Pages | 197-209 |
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Authors | Rowlett RS, Tu C, McKay MM, Preiss JR, Loomis RJ, Hicks KA, Marchione RJ, Strong JA, Donovan GS Jr, Chamberlin JE |
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Title | Kinetic characterization of wild-type and proton transfer-impaired variants of beta-carbonic anhydrase from Arabidopsis thaliana. |
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[10] |
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PubMed ID | 12484784 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 15429-35 |
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Authors | Tu C, Rowlett RS, Tripp BC, Ferry JG, Silverman DN |
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Title | Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class. |
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[11] |
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PubMed ID | 12107142 |
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Journal | J Bacteriol |
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Year | 2002 |
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Volume | 184 |
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Pages | 4240-5 |
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Authors | Smith KS, Ingram-Smith C, Ferry JG |
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Title | Roles of the conserved aspartate and arginine in the catalytic mechanism of an archaeal beta-class carbonic anhydrase. |
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[12] |
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PubMed ID | 15081890 |
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Journal | Arch Biochem Biophys |
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Year | 2004 |
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Volume | 425 |
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Pages | 25-32 |
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Authors | Rowlett RS, Tu C, Murray PS, Chamberlin JE |
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Title | Examination of the role of Gln-158 in the mechanism of CO(2) hydration catalyzed by beta-carbonic anhydrase from Arabidopsis thaliana. |
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comments | This enzyme belongs to the beta-carbonic anhydrase family. The catalytic zinc ion is ligated by two conserved cysteine residues and a conserved histidine, together with a conserved aspartate residue (Asp162 of 1ekj). However, in some structures, the aspartate residue is displaced, suggesting that this residue function as a switch of catalytic reaction (see [8]). According to the literature [4], [7], [8], [9] & [12], the catalytic reaction proceeds as follows: (1) A water molecule is bound to the cofactor zinc. (2) A proton of the substrate water is abstracted by a general base or proton shuttle residue (which transfers a proton to the solvent), or solvent, to generate the hydroxide. This role is probably played by Tyr205' from the adjacent chain (of 1ekj). (Asp162 may act as a general base, which deprotonates the water bound to the cofactor zinc ion.) (3) The hydroxide bound to zinc makes a nucleophilic attack on the carbon atom of another substrate, carbon dioxide (CO2), which is stabilized by Gln151' from the adjacent chain (of 1ekj). The nucleophile, the hydroxide, is also stabilized by Asp162. This reaction leads to the formation of the product, bicarbonate anion.
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created | updated |
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2004-07-15 | 2009-02-26 |
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