Literature summary for 4.2.1.1 extracted from

Duda, D.M.; Tu, C.; Fisher, S.Z.; An, H.; Yoshioka, C.; Govindasamy, L.; Laipis, P.J.; Agbandje-McKenna, M.; Silverman, D.N.; McKenna, R.
Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer (2005), Biochemistry, 44, 10046-10053.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of C-terminal hexahistidine-tagged carbonic anhydrase III and F198L carbonic anhydrase III, hanging-drop vapour diffusion method, 2.1 A resolution	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C183S/C188S	mutations at positions 183 and 188 are to enhance crystallization by removing oxidizable cysteine residues. The positions of residues 183 and 188 are solvent exposed on the side of the enzyme opposite to the active site. The mutations C183S and C188S do not affect catalysis	Homo sapiens
F198L/C183S/C188S	the ratio of turnover-number to Km-value for hydration of CO2 of mutant enzyme F198L/C183S/C188S is 25fold higher than the ratio of wild-type enzyme and mutant enzyme C183S/C188S	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P07451	-	-

Synonyms

Synonyms	Comment	Organism
carbonic anhydrase III	-	Homo sapiens
hCA III	-	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2000	-	CO2	25°C, mutant enzyme C183S/C188S	Homo sapiens
22000	-	CO2	25°C, mutant enzyme F198L/C183S/C188S	Homo sapiens

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Release 2023.1 (January 2023)