NDLI: Metal ion dependency of serine racemase from Dictyostelium discoideum

Content Provider	Springer Nature Link
Author	Ito, Tomokazu Murase, Hirotaka Maekawa, Motoki Goto, Masaru Hayashi, Shuhei Saito, Hajime Maki, Masatoshi Hemmi, Hisashi Yoshimura, Tohru
Copyright Year	2012
Abstract	d-Serine is known to act as an endogenous co-agonist of the N-methyl-d-aspartate receptor in the mammalian brain and is endogenously synthesized from l-serine by a pyridoxal 5′-phosphate-dependent enzyme, serine racemase. Though the soil-living mycetozoa Dictyostelium discoideum possesses no genes homologous to that of NMDA receptor, it contains genes encoding putative proteins relating to the d-serine metabolism, such as serine racemase, d-amino acid oxidase, and d-serine dehydratase. D. discoideum is an attractive target for the elucidation of the unknown functions of d-serine such as a role in cell development. As part of the elucidation of the role of d-serine in D. discoideum, we cloned, overexpressed, and examined the properties of the putative serine racemase exhibiting 46% amino acid sequence similarity with the human enzyme. The enzyme is unique in its stimulation by monovalent cations such as Na+ in addition to Mg2+ and Ca2+, which are well-known activators for the mammalian serine racemase. Mg2+ or Na+ binding caused two- to ninefold enhancement of the rates of both racemization and dehydration. The half-maximal activation concentrations of Mg2+ and Na+ were determined to be 1.2 μM and 2.2 mM, respectively. In the l-serine dehydrase reaction, Mg2+ and Na+ enhanced the k cat value without changing the K m value. Alanine mutation of the residues E207 and D213, which correspond to the Mg2+-binding site of Schizosaccharomyces pombe serine racemase, abolished the Mg2+- and Na+-dependent stimulation. These results suggest that Mg2+ and Na+ share the common metal ion-binding site.
Starting Page	1567
Ending Page	1576
Page Count	10
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	43
Issue Number	4
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2012-02-05
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	d-Serine Serine racemase Dictyostelium discoideum Metal ion activation Proteomics Life Sciences Neurobiology Biochemistry Biochemical Engineering Analytical Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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