Abstract:
:We have cloned and overexpressed a variant of Arabidopsis thaliana beta-carbonic anhydrase (Q158A) that deletes the functional equivalent of the backbone amide NH of Thr-199 in human alpha-carbonic anhydrase II. The latter residue is hypothesized to be important in catalyzing the rate of CO(2)(-) HCO (3)(-) interconversion in alpha-carbonic anhydrase but this hypothesis is not directly testable in that enzyme. Kinetic studies of a variant of the functionally equivalent residue in A. thaliana beta-carbonic anhydrase provide direct evidence for the role of this residue in beta-carbonic anhydrase. Namely, the mutation of Gln-158 to Ala results in a significant decrease in the maximal k(cat) (33% of wild type) at steady state and the maximal rate of CO(2)(-) HCO(2)(-) exchange at chemical equilibrium as measured by R(1)/[E] (7% of wild type), while leaving the maximal rate of H(+) transfer, as measured by k(cat) at steady state, or R(H(2)O)) at chemical equilibrium, largely unaffected.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Rowlett RS,Tu C,Murray PS,Chamberlin JEdoi
10.1016/j.abb.2004.02.033subject
Has Abstractpub_date
2004-05-01 00:00:00pages
25-32issue
1eissn
0003-9861issn
1096-0384pii
S0003986104001213journal_volume
425pub_type
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