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Kinetic study of porcine kidney betaine aldehyde dehydrogenase.

Abstract：

:Porcine kidney betaine aldehyde dehydrogenase (EC 1.2.1.8) kinetic properties were determined at low substrate concentrations. The double-reciprocal plots of initial velocity versus substrate concentration are linear and intersect at the left of the 1/v axis and showed substrate inhibition with betaine aldehyde. Studies of inhibition by NADH and dead-end analogs showed that NADH is a mixed inhibitor against NAD(+) and betaine aldehyde. AMP is competitive with respect to NAD(+) and mixed with betaine aldehyde. Choline is competitive against betaine aldehyde and uncompetitive with respect to NAD(+). The kinetic behavior is consistent with an Iso-Ordered Bi-Bi Steady-State mechanism.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Figueroa-Soto CG,Valenzuela-Soto EM

doi

10.1006/bbrc.2000.2337

subject

Has Abstract

pub_date

2000-03-16 00:00:00

pages

596-603

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92337-4

journal_volume

269

pub_type

杂志文章

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