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Vitamin K-dependent carboxylase from calf liver: studies on the steady-state kinetic mechanism.

Abstract：

:The steady-state kinetic mechanism of vitamin K-dependent carboxylase from calf liver has been investigated by initial-velocity measurements with varying concentrations of two carboxylase substrates and constant, nonsaturating concentrations of the other two substrates. With all combinations of the varied substrates tested linear kinetics were obtained with lines intersecting on the left side of the 1/v axis in double-reciprocal plots. Thus the carboxylase has a sequential reaction mechanism which includes the quinternary complex of the enzyme with its four substrates. A mechanism with the ordered steady-state addition of all substrates to the enzyme accords well with the results. A totally random mechanism was excluded but the alternative possibility remained that part of the substrates are added in a rapid-equilibrium random reaction. Experiments with saturating constant concentrations of sodium bicarbonate and varying concentrations of the other substrates suggest that bicarbonate (CO2) is either the first or, more probably, the last substrate bound to the enzyme.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Uotila L

doi

10.1016/0003-9861(88)90578-4

subject

Has Abstract

pub_date

1988-07-01 00:00:00

pages

135-43

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90578-4

journal_volume

264

pub_type

杂志文章

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