The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.

Abstract:

:In the first committed reaction of chlorophyll biosynthesis, magnesium chelatase couples ATP hydrolysis to the thermodynamically unfavorable Mg(2+) insertion into protoporphyrin IX (ΔG°' of circa 25-33 kJ·mol(-1) ). We explored the thermodynamic constraints on magnesium chelatase and demonstrate the effect of nucleotide hydrolysis on both the reaction kinetics and thermodynamics. The enzyme produces a significant rate enhancement (kcat /kuncat of 400 × 10(6) m) and a catalytic rate enhancement, kcat/KmDIXK0.5Mgkuncat, of 30 × 10(15) m(-1) , increasing to 300 × 10(15) m(-1) with the activator protein Gun4. This is the first demonstration of the thermodynamic benefit of ATP hydrolysis in the AAA(+) family.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Adams NB,Brindley AA,Hunter CN,Reid JD

doi

10.1002/1873-3468.12214

subject

Has Abstract

pub_date

2016-06-01 00:00:00

pages

1687-93

issue

12

eissn

0014-5793

issn

1873-3468

journal_volume

590

pub_type

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