Literature summary for 4.2.1.1 extracted from

Maupin, C.M.; Zheng, J.; Tu, C.; McKenna, R.; Silverman, D.N.; Voth, G.A.
Effect of active-site mutation at Asn67 on the proton transfer mechanism of human carbonic anhydrase II (2009), Biochemistry, 48, 7996-8005.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N67L	the hydrogen-bonding network is disruptedin the active site of the N67L mutant, shows inability to stabilize water clusters when His64 is in the inward orientation, thereby favoring proton transfer when His64 is in the outward orientation	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc-metalloenzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00918	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant enzyme N67L is purified by affinity chromatography using 4-(aminomethyl)benzenesulfonamide coupled to agarose beads	Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

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

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Release 2023.1 (January 2023)