Value |
1e+6
1/sec
|
Organism |
Pea Pisum sativum |
Reference |
Lindskog S. Structure and mechanism of carbonic anhydrase. Pharmacol Ther. 1997 74(1):pp. 2PubMed ID9336012
|
Primary Source |
Johansson IM, Forsman C. Solvent hydrogen isotope effects and anion inhibition of CO2 hydration catalysed by carbonic anhydrase from Pisum sativum. Eur J Biochem. 1994 Sep 15 224(3):901-7.PubMed ID7925414
|
Method |
cDNA encoding pea carbonic anhydrase was isolated and cloned into a mutagenesis expression vector giving the plasmid pPCA. Initial rates of CO2 hydration were measured in a hi-tech stopped-flow spectrophotometer at 25 degrees c by the changing pH-indicator method |
Comments |
A Kcat value of 10^6 1/sec was calculated for the subunit of the pea enzyme upon extrapolation to infinite concentrations of barbital buffer |
Entered by |
Uri M |
ID |
102672 |