Literature summary for 4.2.1.1 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Chlamydomonas reinhardtii	-	isozyme alphaCA1	-

Purification (Commentary)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
alphaCA1	-	Chlamydomonas reinhardtii
carbonic anhydrase	-	Chlamydomonas reinhardtii

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Release 2023.1 (January 2023)