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Literature summary extracted from

  • Suzuki, K.; Shimizu, S.; Juan, E.C.; Miyamoto, T.; Fang, Z.; Hoque, M.M.; Sato, Y.; Tsunoda, M.; Sekiguchi, T.; Takenaka, A.; Yang, S.Y.
    Crystallographic study of wild-type carbonic anhydrase alpha CA1 from Chlamydomonas reinhardtii (2010), Acta Crystallogr. Sect. F, 66, 1082-1085.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.1 purified native isozyme alphaCA1, 0.002 ml of 20 mg/ml protein in 25 mM Tris-HCl, pH 7.5, is mixed with 0.002 ml of reservoir solution, containing 1.0 M ammonium sulfate and 100 mM Tris-HCl, pH 8.5, and equilibrated against 0.7 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.88 A resolution, MAD method Chlamydomonas reinhardtii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Zn2+ two Zn atoms in the alphaCA1 crystal asymmetric unit Chlamydomonas reinhardtii

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Chlamydomonas reinhardtii
-
 isozyme alphaCA1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.1 native enzyme by anion exchange and hydrophobic interaction chromatography, followed by gel filtration Chlamydomonas reinhardtii

Subunits

EC Number Subunits Comment Organism
4.2.1.1 dimer most alphaCA enzymes are monomeric, but alphaCA1 from Chlamydomonas reinhardtii is a dimer that is uniquely stabilized by disulfide bonds, crystal structure determination and analysis Chlamydomonas reinhardtii

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 alphaCA1
-
 Chlamydomonas reinhardtii
4.2.1.1 carbonic anhydrase
-
 Chlamydomonas reinhardtii