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The a subunit ala-217 --> arg substitution affects catalytic activity of F(1)F(0) ATP synthase.

Abstract：

:A large number of mutations affecting the F(0) sector of Escherichia coli F(1)F(0) ATP synthase have been constructed and characterized. A subset of the missense mutations resulted in fully assembled enzyme complexes blocked in proton translocation and displaying marked decreases in ATP hydrolysis activity. The catalytic activities of one such mutant enzyme, a(ala-217-->arg), have been determined using both multisite and unisite catalysis conditions. As expected, the V(max) of the a(ala-217-->arg) enzyme was reduced under conditions of saturating substrate concentration. However, the F(0) sector amino acid substitution did not affect nucleotide occupancy of the noncatalytic sites. Moreover, the microscopic rate constants measured using unisite methods yielded no significant differences between the intact wild type F(1)F(0) ATP synthase and the a(ala-217-->arg) mutant enzyme. In general, the values for unisite activities in both preparations were very similar to numbers reported in the literature for E. coli F(1)-ATPase. The results suggest that the a(ala-217-->arg) substitution resulted in a defect in catalytic cooperativity and most likely altered the enzyme by inhibiting the rotational mechanism of F(1)F(0) ATP synthase.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Gardner JL,Cain BD

doi

10.1006/abbi.2000.1916

subject

Has Abstract

pub_date

2000-08-01 00:00:00

pages

201-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(00)91916-7

journal_volume

380

pub_type

杂志文章

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