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Literature summary extracted from

  • Simler, B.R.; Doyle, B.L.; Matthews, C.R.
    Zinc binding drives the folding and association of the homo-trimeric gamma-carbonic anhydrase from Methanosarcina thermophila (2004), Protein Eng. Des. Sel., 17, 285-291.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.1 expression in Escherichia coli Methanosarcina thermophila

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.1 C148S the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148 Methanosarcina thermophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.1 Zn2+ the enzyme binds three catalytic Zn2+ ions at symmetry-related subunit interfaces. Zinc binding drives the folding and association of the homotrimeric enzyme Methanosarcina thermophila

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.1 Zn2+ the individual subunits are only weakly folded and fractionally associated in the absence of Zn2+. The crucial thermodynamic step in the assembly of the trimeric holo-Cam is the incorporation of the three Zn2+ ions, events which must occur after the monomer is resident on the surface and has access to other monomers Methanosarcina thermophila

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.1 Methanosarcina thermophila
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.1
-
 Methanosarcina thermophila

Subunits

EC Number Subunits Comment Organism
4.2.1.1 homotrimer
-
 Methanosarcina thermophila

Synonyms

EC Number Synonyms Comment Organism
4.2.1.1 gamma-carbonic anhydrase
-
 Methanosarcina thermophila