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Literature summary for 4.2.1.1 extracted from

  • Duda, D.; Tu, C.; Qian, M.; Laipis, P.; Agbandje-McKenna, M.; Silverman, D.N.; McKenna, R.
    Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II (2001), Biochemistry, 40, 1741-1748.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type HCA II and H64A II expressed in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant H64A, crystals produced by the hanging drop method, space group P2(1) with unit cell parameters of a : 42.5 A, b : 41.6 A, c : 72.7 A Homo sapiens

Protein Variants

Protein Variants Comment Organism
H64A catalytic activity decreases more than 10fold Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2CO3 Homo sapiens
-
CO2 + H2O
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens P00918
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzymes Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
Homo sapiens CO2 + H2O
-
r

Synonyms

Synonyms Comment Organism
carbonic anhydrase II
-
Homo sapiens
H64A HCA II
-
Homo sapiens
HCA II
-
Homo sapiens
human carbonic anhydrase II
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
5 9
-
Homo sapiens