Literature summary for 4.2.1.1 extracted from

Fisher, S.Z.; Tu, C.; Bhatt, D.; Govindasamy, L.; Agbandje-McKenna, M.; McKenna, R.; Silvermann, D.N.
Speeding up proteon transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II (2007), Biochemistry, 46, 3803-3813.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzymes Y7F, N62L, and N67L in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of the HCA II single-site mutants Y7F, N62L, and N67L are obtained using the hanging-drop vapor diffusion method. All crystals are isomorphous and belong to space group P2(1) with mean unit cell dimensions: a = 42.7 A, b = 41.6 A, c = 72.9 A and beta = 104.6°	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N67L	turnover-number for hydration is 1.4fold lower than wild-type value. Turnover-number for dehydration is 5.8fold lower than wild-type value	Homo sapiens
Y7F	turnover-number for hydration is identical to wild-type value. Turnover-number for dehydration is 5.8fold lower than wild-type value	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00918	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CO2 + H2O	roles for residues 7, 62, and 67 in finetuning the properties of His64 for optimal proton transfer in catalysis	Homo sapiens	H2CO3	-	?

Synonyms

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

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Release 2023.1 (January 2023)