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Literature summary for 4.2.1.1 extracted from

  • Liu, Z.; Bartlow, P.; Dilmore, R.M.; Soong, Y.; Pan, Z.; Koepsel, R.; Ataai, M.
    Production, purification, and characterization of a fusion protein of carbonic anhydrase from Neisseria gonorrhoeae and cellulose binding domain from Clostridium thermocellum (2009), Biotechnol. Prog., 25, 68-74.
    View publication on PubMed
Search for more literature for 4.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Neisseria gonorrhoeae

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-containing enzyme Neisseria gonorrhoeae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 SDS-PAGE Neisseria gonorrhoeae

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Neisseria gonorrhoeae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO2 + H2O
-
 Neisseria gonorrhoeae H2CO3
-
 r

Synonyms

Synonyms Comment Organism
carbonic anhydrase
-
 Neisseria gonorrhoeae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3133
-
 CO2 purified recombinant enzyme Neisseria gonorrhoeae