Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana☆

Fujitani, Yoshiyuki; Nakajima, Nobuyoshi; Koji, Ishihara; Oikawa, Tadao; Ito, Kazutoshi; Sugimoto, Mineharu

doi:10.1016/j.phytochem.2006.01.003

Cited by 50 publications

(53 citation statements)

References 31 publications

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“…There is no previous report on a plant D-amino acid oxidase, and the serine racemase is the only known enzyme that degrades 1a in plants. The specific activities of racemization and dehydration for 1b were as follows: 14 and 228 nmol/min/mg with regard to HvSR, 10 and 214 nmol/min/mg with regard to OsSR, and 4.1 and 86 nmol/min/mg with regard to AtSR (Fujitani et al, 2006), respectively: the corresponding dehydratase activities were about 20-fold higher than racemase activity. This is as contrast to the dehydration/racemization ratio of about 0.7 for mouse serine racemase (De Miranda et al, 2002).…”

Section: Discussionmentioning

confidence: 89%

“…Fe 2+ inhibits racemase activity of HvSR whereas that of AtSR is slightly increased by addition of Fe 2+ (Fujitani et al, 2006). While the combined effect of Mg 2+ and ATP on mouse serine racemase leads to an increase in 1a production, there was no synergy between Mg 2+ and ATP on HvSR activity, as with AtSR.…”

Section: Discussionmentioning

confidence: 90%

“…The deduced amino acid sequence of HvSR showed 89% identity with that of a putative rice serine racemase in data banks (OsSR, AL606647), and 68, 46, 45, and 28% identity with a serine racemase from A. thaliana (AtSR, AB206823, Fujitani et al, 2006), as well as human (hSR, AF169974, De Miranda et al, 2000) and mouse (mSR, AF148321, Wolosker et al, 1999) serine racemases, and catalytic domain of L-threonine dehydratase from Escherichia coli (EcTD, Swiss-Plot no. Gallagher, et al, 1998), respectively.…”

Section: Sequence Analysis Of Barley Serine Racemasementioning

confidence: 99%

“…The serine racemase and dehydratase activities were assayed by calculating the hydroxyperoxide production with amino acid oxidase-peroxidase-OPA and by calculating the pyruvate production with 2,4-dinitrophenylhydrazine, respectively, according to the method described previously (Fujitani et al, 2006).…”

Section: Enzyme and Protein Assaysmentioning

confidence: 99%

“…al., 1977), barley grain, hops blossoms (Erbe and Bruckner, 2000), and tobacco leaves (Kullman et al, 1999). Recently, a serine racemase gene was cloned from Arabidopsis thaliana and expressed to produce a protein that has both racemase and dehydratase activities (Fujitani et al, 2006). This gene also has 46 and 45% identity to human and mouse serine racemases, respectively, and the pyridoxal 5-phosphate (PLP)-binding domain is conserved as with mammalian serine racemases.…”

Section: Introductionmentioning

confidence: 99%

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Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: Gene cloning and recombinant protein characterization☆

et al. 2007

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Several D-amino acids have been identified in plants. However, the biosynthetic pathway to them is unclear.In this study, we cloned and sequenced a cDNA encoding a serine racemase from barley which contained an open reading frame encoding 337 amino acid residues. The deduced amino acid sequence showed significant identity to plant and mammalian serine racemases and contained conserved pyridoxal 5-phosphate (PLP)-binding lysine and PLP-interacting amino acid residues. The purified gene product catalyzed not only racemization of serine but also dehydration of serine to pyruvate. The enzyme requires PLP and divalent cations such as Ca 2+ , Mg 2+ , or Mn 2+ , but not ATP, whereas mammalian serine racemase activity is increased by ATP. In addition to the results regarding the effect of ATP on enzyme activity and the phylogenetic analysis of eukaryotic serine racemases, the antiserum against Arabidopsis serine racemase did not form a precipitate with barley and rice serine racemases. This suggests that plant serine racemases represent a distinct group in the eukaryotic serine racemase family and can be clustered into monocot and dicot types.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 90%

Section: Sequence Analysis Of Barley Serine Racemasementioning

confidence: 99%

Section: Enzyme and Protein Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: Gene cloning and recombinant protein characterization☆

et al. 2007

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d‐Amino acids in biological systems

Wey

Armstrong

2023

Chirality

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Investigations on the occurrence and biochemical roles of free D‐amino acids and D‐amino acid‐containing peptides and proteins in living systems have increased in frequency and significance. Their occurrence and roles may vary substantially with progression from microbiotic to evermore advanced macrobiotic systems. We now understand many of the biosynthetic and regulatory pathways, which are outlined herein. Important uses for D‐amino acids in plants, invertebrates, and vertebrates are reviewed. Given its importance, a separate section on the occurrence and role of D‐amino acids in human disease is presented.

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Assay of Amino Acid Racemases

Katane

Sekine

Homma

2011

Methods in Molecular Biology

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D-Amino acids play important physiological roles in the mammalian body. Recent investigations revealed that, in mammals, D-amino acids are synthesized from their corresponding L-enantiomers via amino acid racemase. This article describes a method used to measure amino acid racemase activity by high-performance liquid chromatography (HPLC). The assay involves fluorogenic chiral derivatization of amino acids with a newly developed reagent, and enantioseparation of D- and L-amino acid derivatives by HPLC. The method is accurate and reliable, and can be automated using a programmable autosampling injector.

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Molecular and biochemical characterization of a serine racemase from Arabidopsis thaliana☆

Cited by 50 publications

References 31 publications

Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: Gene cloning and recombinant protein characterization☆

Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: Gene cloning and recombinant protein characterization☆

d‐Amino acids in biological systems

Assay of Amino Acid Racemases

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