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Literature summary for 4.2.1.1 extracted from

  • Domsic, J.F.; Williams, W.; Fisher, S.Z.; Tu, C.; Agbandje-McKenna, M.; Silverman, D.N.; McKenna, R.
    Structural and kinetic study of the extended active site for proton transfer in human carbonic anhydrase II (2010), Biochemistry, 49, 6394-6399.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant K170 HCA II variants, hanging drop vapour diffusion method, 2-3days, X-ray diffraction structure determination at room temperature and analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
K170A site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II Homo sapiens
K170D site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II Homo sapiens
K170E site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II Homo sapiens
K170H site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required for catalysis, the side chain of His64 occupies two conformations in wild-type HCA II, pointing inward toward the zinc or outward toward bulk solvent 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by affinity chromatography on a 4-(aminomethyl)-benzene-sulfonamide resin Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2CO3
-
 Homo sapiens CO2 + H2O
-
 r
H2CO3 the proton transfer from a zinc-bound water molecule to the proton shuttle His64, along a hydrogen-bonded water network, limits the reaction velocity of CO2 hydration. The side chain of His64 occupies two conformations in wild-type HCA II, pointing inward toward the zinc or outward toward bulk solvent. The enzyme shows a significant extension of the effective active site of HCA II from the zinc-bound water at the base of the conical cavity in the enzyme to Lys170 near the rim of the cavity Homo sapiens CO2 + H2O
-
 r
additional information the enzyme also shows esterase activity in 4-nitrophenylacetate hydrolysis Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
carbonic anhydrase II
-
 Homo sapiens