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The role of Cys271 in conformational changes of arginine kinase.

Abstract：

:Arginine kinase (AK), a crucial enzyme in energy metabolism, buffers cellular ATP levels by catalyzing the reversible phosphoryl transfer between ATP and arginine. To better understand the role of Cys271 in conformational changes of AK from greasyback shrimp (Metapenaeus ensis), we replaced the residue with serine and alanine. A detailed comparison of the catalytic activity and conformation was made between wild-type AK and the mutants by means of activity analysis, ultraviolet (UV) difference, fluorescence spectrum and size exclusion chromatography (SEC). The results indicated that the catalytic activity of the two mutants was gone. The substrates, arginine-ADP-Mg(2+) could induce conformational changes, and additional NO(3)(-) could induce further changes in both the native enzyme and the variants. We speculated that Cys271 might be located in the hinge region between the two domains of AK and cause enzyme conformational changes upon addition of substrate.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Liu N,Wang JS,Wang WD,Pan JC

doi

10.1016/j.ijbiomac.2011.04.002

subject

Has Abstract

pub_date

2011-07-01 00:00:00

pages

98-102

issue

1

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(11)00127-9

journal_volume

49

pub_type

杂志文章

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