Characterization of arginine decarboxylase from Dianthus caryophyllus

Ha, Byung Hak; Cho, Ki Joon; Choi, Yu Jin; Park, Ky Young; Kim, Kyung Hyun

doi:10.1016/j.plaphy.2004.02.001

Cited by 8 publications

(1 citation statement)

References 25 publications

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“…In silico analysis predicts three putative CuAOs (At1g31670, At1g31710 and At4g12290) are plastidial (A score of 5 was allocated to these three CuAOs using WoLF PSORT online software). Arabidopsis ADC1 (At2g16500), ADC2 (At4g34710), AIH (At5g08170) and CPAH (At2g27450) have been extensively characterized 43 44 45 . Abbreviations: ABAL, 4-aminobutanal; ADC, arginine decarboxylase; ALDH, aldehyde dehydrogenase; Agm, agmatine; AIH, agmatine iminohydrolase; Arg, arginine; Carbamoyl-Put, N -carbamoylputrescine; CPAH, N-carbamoylputrescine amidohydrolase; CuAO, copper amine oxidase; GABA, 4-aminobutrate; GAD, glutamate decarboxylase; PAO, polyamine oxidase; Put, putrescine; Spd, spermidine; Spm, spermine.…”

Section: Figurementioning

confidence: 99%

Arabidopsis aldehyde dehydrogenase 10 family members confer salt tolerance through putrescine-derived 4-aminobutyrate (GABA) production

Zarei

Trobacher

Shelp

2016

Sci Rep

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Polyamines represent a potential source of 4-aminobutyrate (GABA) in plants exposed to abiotic stress. Terminal catabolism of putrescine in Arabidopsis thaliana involves amine oxidase and the production of 4-aminobutanal, which is a substrate for NAD+-dependent aminoaldehyde dehydrogenase (AMADH). Here, two AMADH homologs were chosen (AtALDH10A8 and AtALDH10A9) as candidates for encoding 4-aminobutanal dehydrogenase activity for GABA synthesis. The two genes were cloned and soluble recombinant proteins were produced in Escherichia coli. The pH optima for activity and catalytic efficiency of recombinant AtALDH10A8 with 3-aminopropanal as substrate was 10.5 and 8.5, respectively, whereas the optima for AtALDH10A9 were approximately 9.5. Maximal activity and catalytic efficiency were obtained with NAD+ and 3-aminopropanal, followed by 4-aminobutanal; negligible activity was obtained with betaine aldehyde. NAD+ reduction was accompanied by the production of GABA and β-alanine, respectively, with 4-aminobutanal and 3-aminopropanal as substrates. Transient co-expression systems using Arabidopsis cell suspension protoplasts or onion epidermal cells and several organelle markers revealed that AtALDH10A9 was peroxisomal, but AtALDH10A8 was cytosolic, although the N-terminal 140 amino acid sequence of AtALDH10A8 localized to the plastid. Root growth of single loss-of-function mutants was more sensitive to salinity than wild-type plants, and this was accompanied by reduced GABA accumulation.

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Section: Figurementioning

confidence: 99%

Arabidopsis aldehyde dehydrogenase 10 family members confer salt tolerance through putrescine-derived 4-aminobutyrate (GABA) production

Zarei

Trobacher

Shelp

2016

Sci Rep

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Dianthus caryophyllus

Lim¹

2013

Edible Medicinal and Non-Medicinal Plants

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Expression and purification of recombinant arginine decarboxylase (speA) from Escherichia coli

Song

Zhou

et al. 2009

Mol Biol Rep

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The crystal structures of almost all the enzymes of arginine metabolism have been determined, but arginine decarboxylase's structure is not resolved yet. In order to characterize and crystallize arginine decarboxylase, we overexpressed biosynthetic arginine decarboxylase (ADC; EC 4.1.1.19, encoded by the speA gene) from Escherichia coli in the T7 expression system as a cleavable poly-His-tagged fusion construct. The expressed recombinant His(10)-ADC (77.3 kDa) was first purified by Ni-NTA affinity chromatography, then proteolytically digested with Tobacco Etch Virus (TEV) protease to remove the poly-His fusion tag, and finally purified by anion exchange chromatography. The His(10) tag removed recombinant ADC (74.1 kDa)'s typical yield was 90 mg from 1 l of culture medium with purity above 98%. The recombinant ADC was assayed for decarboxylase activity, showing decarboxylase activity of 2.8 U/mg, similar to the purified native E. coli ADC. The decarboxylase activity assay also showed that the purified recombinant ADC tolerated broad ranges of pH (pH 6-9) and temperature (20-80 degrees C). Our research may facilitate further studies of ADC structure and function, including the determination of its crystal structure by X-ray diffraction.

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Characterization of arginine decarboxylase from Dianthus caryophyllus

Cited by 8 publications

References 25 publications

Arabidopsis aldehyde dehydrogenase 10 family members confer salt tolerance through putrescine-derived 4-aminobutyrate (GABA) production

Arabidopsis aldehyde dehydrogenase 10 family members confer salt tolerance through putrescine-derived 4-aminobutyrate (GABA) production

Dianthus caryophyllus

Expression and purification of recombinant arginine decarboxylase (speA) from Escherichia coli

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