Literature summary for 4.2.1.1 extracted from

Elder, I.; Fisher, Z.; Laipis, P.J.; Tu, C.; McKenna, R.; Silverman, D.N.
Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III (2007), Proteins, 68, 337-343.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of K64H, R67H, and K64H/R67N HCA III are grown by hanging drop vapor diffusion method. X-ray crystal structures of site-specific mutants of human carbonic anhydrase III (HCA III): K64H, R67H, and K64H/R67N HCA III	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
K64H	mutant has enhanced proton transfer in catalysis compared with wild-type HCA III	Homo sapiens
K64H/R67N	mutant has enhanced proton transfer in catalysis compared with wild-type HCA III	Homo sapiens
R67H	mutant has enhanced proton transfer in catalysis compared with wild-type HCA III	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P07451	-	-

Synonyms

Synonyms	Comment	Organism
carbonic anhydrase III	-	Homo sapiens

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Release 2023.1 (January 2023)