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Literature summary for 4.2.1.1 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)

Cloned (Comment) Organism
expression in Escherichia coli Methanosarcina thermophila

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Methanosarcina thermophila
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanosarcina thermophila

Subunits

Subunits Comment Organism
homotrimer
-
Methanosarcina thermophila

Synonyms

Synonyms Comment Organism
gamma-carbonic anhydrase
-
Methanosarcina thermophila